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Conserved domains on  [gi|1737379514|emb|VAK76672|]
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protein YibD [Enterobacter cloacae]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10455355)

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|10521532|12691742|12200473|10508766
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-172 7.50e-25

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: 97.85  E-value: 7.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   5 SIIIAAHNAEDTLHTTLESLhdaIDNAGDDVEVIIFNDSSDDSTQDIIETWLPAFPNVHSRHVQfRNVGLV--RNSAFSL 82
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESL---LNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLP-ENRGKAgaRNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514  83 ASGDYITMLDSDDRLKPGSIRDAVAFLKTERPDM-LLTRLLEIRDIKKITPNWQGFSPVALSQREAIKRFLLHKDFQAHL 161
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVvVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGF 156

                         170
                  ....*....|.
gi 1737379514 162 IGqfIHRKLYE 172
Cdd:pfam00535 157 AL--YRREALE 165
 
Name Accession Description Interval E-value
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-172 7.50e-25

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: 97.85  E-value: 7.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   5 SIIIAAHNAEDTLHTTLESLhdaIDNAGDDVEVIIFNDSSDDSTQDIIETWLPAFPNVHSRHVQfRNVGLV--RNSAFSL 82
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESL---LNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLP-ENRGKAgaRNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514  83 ASGDYITMLDSDDRLKPGSIRDAVAFLKTERPDM-LLTRLLEIRDIKKITPNWQGFSPVALSQREAIKRFLLHKDFQAHL 161
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVvVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGF 156

                         170
                  ....*....|.
gi 1737379514 162 IGqfIHRKLYE 172
Cdd:pfam00535 157 AL--YRREALE 165
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-218 1.02e-24

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 98.62  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   1 MAFLSIIIAAHNAEDTLHTTLESLHDAIdnaGDDVEVIIFNDSSDDSTQDIIETWLPAFPNVHS-RHVQFRNVGLVRNSA 79
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQT---YPDFEIIVVDDGSTDGTAEILRELAAKDPRIRViRLERNRGKGAARNAG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514  80 FSLASGDYITMLDSDDRLKPGSIRDAVAFLKTERPDMLLTRlleiRDIKKITPNWQGFSPVALSqreAIKRFLLHKDFQA 159
Cdd:COG0463    78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGS----RLIREGESDLRRLGSRLFN---LVRLLTNLPDSTS 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1737379514 160 HLigQFIHRKLYESNPIPsmvcyEDFAVFPGMLMQSSKIAYQRRGHYYYIKRSDSLSSK 218
Cdd:COG0463   151 GF--RLFRREVLEELGFD-----EGFLEDTELLRALRHGFRIAEVPVRYRAGESKLNLR 202
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-113 4.75e-20

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: 84.87  E-value: 4.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   6 IIIAAHNAEDTLHTTLESLHDAIDnagDDVEVIIFNDSSDDSTQDIIETWLPAFPNVHSRHVQ-FRNVGLVRNSAFSLAS 84
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTY---PNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEeNQGLAAARNAGLKAAR 77

                          90       100
                  ....*....|....*....|....*....
gi 1737379514  85 GDYITMLDSDDRLKPGSIRDAVAFLKTER 113
Cdd:cd00761    78 GEYILFLDADDLLLPDWLERLVAELLADP 106
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 4-100 3.39e-16

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 77.39  E-value: 3.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   4 LSIIIAAHNAEDTLHTTLESLhdaIDNAGDDVEVIIFNDSSDDSTQDIIETWLPAFPNVHSRHVQFRNVGLVRNSAFSLA 83
Cdd:PRK10073    8 LSIIIPLYNAGKDFRAFMESL---IAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTGLAVA 84

                          90
                  ....*....|....*..
gi 1737379514  84 SGDYITMLDSDDRLKPG 100
Cdd:PRK10073   85 TGKYVAFPDADDVVYPT 101
 
Name Accession Description Interval E-value
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-172 7.50e-25

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: 97.85  E-value: 7.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   5 SIIIAAHNAEDTLHTTLESLhdaIDNAGDDVEVIIFNDSSDDSTQDIIETWLPAFPNVHSRHVQfRNVGLV--RNSAFSL 82
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESL---LNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLP-ENRGKAgaRNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514  83 ASGDYITMLDSDDRLKPGSIRDAVAFLKTERPDM-LLTRLLEIRDIKKITPNWQGFSPVALSQREAIKRFLLHKDFQAHL 161
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVvVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGF 156

                         170
                  ....*....|.
gi 1737379514 162 IGqfIHRKLYE 172
Cdd:pfam00535 157 AL--YRREALE 165
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-218 1.02e-24

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 98.62  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   1 MAFLSIIIAAHNAEDTLHTTLESLHDAIdnaGDDVEVIIFNDSSDDSTQDIIETWLPAFPNVHS-RHVQFRNVGLVRNSA 79
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQT---YPDFEIIVVDDGSTDGTAEILRELAAKDPRIRViRLERNRGKGAARNAG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514  80 FSLASGDYITMLDSDDRLKPGSIRDAVAFLKTERPDMLLTRlleiRDIKKITPNWQGFSPVALSqreAIKRFLLHKDFQA 159
Cdd:COG0463    78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGS----RLIREGESDLRRLGSRLFN---LVRLLTNLPDSTS 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1737379514 160 HLigQFIHRKLYESNPIPsmvcyEDFAVFPGMLMQSSKIAYQRRGHYYYIKRSDSLSSK 218
Cdd:COG0463   151 GF--RLFRREVLEELGFD-----EGFLEDTELLRALRHGFRIAEVPVRYRAGESKLNLR 202
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-113 4.75e-20

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: 84.87  E-value: 4.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   6 IIIAAHNAEDTLHTTLESLHDAIDnagDDVEVIIFNDSSDDSTQDIIETWLPAFPNVHSRHVQ-FRNVGLVRNSAFSLAS 84
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTY---PNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEeNQGLAAARNAGLKAAR 77

                          90       100
                  ....*....|....*....|....*....
gi 1737379514  85 GDYITMLDSDDRLKPGSIRDAVAFLKTER 113
Cdd:cd00761    78 GEYILFLDADDLLLPDWLERLVAELLADP 106
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 1-116 1.15e-19

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: 87.10  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   1 MAFLSIIIAAHNAEDTLHTTLESLHdAIDNAGDDVEVIIFNDSSDDSTQDIIETWLPAFPNVHSRHVQFR-NVGLVRNSA 79
Cdd:COG1215    28 LPRVSVIIPAYNEEAVIEETLRSLL-AQDYPKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENgGKAAALNAG 106

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1737379514  80 FSLASGDYITMLDSDDRLKPGSIRDAVAFLKTERPDM 116
Cdd:COG1215   107 LKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGA 143
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 6-109 2.77e-17

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 78.04  E-value: 2.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   6 IIIAAHNAEDTLHTTLESLHdAIDNagDDVEVIIFNDSSDDSTQDIIETWLPAFPNVHSRHVQFRNVGLVR--NSAFSLA 83
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLL-ALDY--PKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGGKAGalNAGLRHA 77

                          90       100
                  ....*....|....*....|....*.
gi 1737379514  84 SGDYITMLDSDDRLKPGSIRDAVAFL 109
Cdd:cd06423    78 KGDIVVVLDADTILEPDALKRLVVPF 103
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 4-100 3.39e-16

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 77.39  E-value: 3.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   4 LSIIIAAHNAEDTLHTTLESLhdaIDNAGDDVEVIIFNDSSDDSTQDIIETWLPAFPNVHSRHVQFRNVGLVRNSAFSLA 83
Cdd:PRK10073    8 LSIIIPLYNAGKDFRAFMESL---IAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTGLAVA 84

                          90
                  ....*....|....*..
gi 1737379514  84 SGDYITMLDSDDRLKPG 100
Cdd:PRK10073   85 TGKYVAFPDADDVVYPT 101
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-108 1.27e-15

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 73.87  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   1 MAFLSIIIAAHNAEDTLHTTLESLhdaIDNAGDDVEVIIFNDSSDDSTQDIIETWlpAFPNVHsRHVQFRNVGLV--RNS 78
Cdd:COG1216     2 RPKVSVVIPTYNRPELLRRCLESL---LAQTYPPFEVIVVDNGSTDGTAELLAAL--AFPRVR-VIRNPENLGFAaaRNL 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 1737379514  79 AFSLASGDYITMLDSDDRLKPGSIRDAVAF 108
Cdd:COG1216    76 GLRAAGGDYLLFLDDDTVVEPDWLERLLAA 105
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 4-115 2.21e-13

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: 68.08  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   4 LSIIIAAHNAEDTLHTTLESLHDAIDnagddvEVIIFNDSSDDSTQDIIEtwlpaFPNVHSRHVQFRNVGLVRNSAFSLA 83
Cdd:cd02511     2 LSVVIITKNEERNIERCLESVKWAVD------EIIVVDSGSTDRTVEIAK-----EYGAKVYQRWWDGFGAQRNFALELA 70

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1737379514  84 SGDYITMLDSDDRLKPGSIRDAVAFLKTERPD 115
Cdd:cd02511    71 TNDWVLSLDADERLTPELADEILALLATDDYD 102
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 4-120 2.38e-13

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 68.17  E-value: 2.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   4 LSIIIAAHNAEDTLHTTLESLhdaIDNAGDDVEVIIFNDSSDDSTQDIIETWLPAFPNVHSRHVQFRNVGLVR------N 77
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAI---LAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTgksrglN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1737379514  78 SAFSLASGDYITMLDSDDRLKPGSIRDAVAFLKTERPDMLLTR 120
Cdd:pfam13641  81 HGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTP 123
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 6-116 5.36e-13

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: 66.06  E-value: 5.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   6 IIIAAHNAEDTLHTTLESLHDAIDnAGDDVEVIIFNDSSDDSTQDIIETWLPAFPNVhsRHVQF-RNVGL---VRnSAFS 81
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLE-EGYDYEIIVVDDGSTDGTAEIARELAARVPRV--RVIRLsRNFGKgaaVR-AGFK 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1737379514  82 LASGDYITMLDSDDRLKPGSIRDAVAFLKTERPDM 116
Cdd:cd04179    77 AARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADV 111
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 6-122 1.18e-11

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic 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. 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. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 62.11  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   6 IIIAAHNAEDTLHTTLESLHDAIDNAGDDVEVIIFNDSSDDSTQDIIETWLPAFPNVhsRHVQF-RNVGLVRN--SAFSL 82
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRV--KVIRLsRNFGQQAAllAGLDH 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1737379514  83 ASGDYITMLDSD------------DRLKPGSirDAVAFLKTERPDMLLTRLL 122
Cdd:cd04187    79 ARGDAVITMDADlqdppelipemlAKWEEGY--DVVYGVRKNRKESWLKRLT 128
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 5-107 1.36e-11

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 63.37  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   5 SIIIAAHNAEDTLHTTLESLHdAIDNAGDDVEVIIFNDSSDDSTQDIIETWLPafPNVHsRHVQFRNVGLVR--NSAFSL 82
Cdd:cd06439    32 TIIIPAYNEEAVIEAKLENLL-ALDYPRDRLEIIVVSDGSTDGTAEIAREYAD--KGVK-LLRFPERRGKAAalNRALAL 107

                          90       100
                  ....*....|....*....|....*
gi 1737379514  83 ASGDYITMLDSDDRLKPGSIRDAVA 107
Cdd:cd06439   108 ATGEIVVFTDANALLDPDALRLLVR 132
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-118 1.94e-11

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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 62.69  E-value: 1.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   6 IIIAAHNAEDTLHTTLESLhDAIDNAGDDVEVIIFNDSSDDSTQDIIEtWLPAFPNVHSRHVQFRNVGLVR-----NSAF 80
Cdd:cd04192     1 VVIAARNEAENLPRLLQSL-SALDYPKEKFEVILVDDHSTDGTVQILE-FAAAKPNFQLKILNNSRVSISGkknalTTAI 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1737379514  81 SLASGDYITMLDSDDRLKPGSIRDAVAFLKTERPDMLL 118
Cdd:cd04192    79 KAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVA 116
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 3-110 2.11e-11

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 62.63  E-value: 2.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   3 FLSIIIAAHNAEDTLHTTLESLHdAIDNAGDDVEVIIFNDSSDDSTQDIIETWLPAFPNVHSRHVQFRNVGLVRNSAFSL 82
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLL-NQSYPKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNPKRIQSAGLNIGIRN 79

                          90       100
                  ....*....|....*....|....*...
gi 1737379514  83 ASGDYITMLDSDDRLKPGSIRDAVAFLK 110
Cdd:cd02525    80 SRGDIIIRVDAHAVYPKDYILELVEALK 107
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 6-104 5.16e-11

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 61.32  E-value: 5.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   6 IIIAAHNAEDTLHTTLESLHDAiDNAGDdVEVIIFNDSSDDSTQDIIETWLPAFPNV-------HSRHVQFRNVGLVRNS 78
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQ-DFEGT-LELSVFNDASTDKSAEIIEKWRKKLEDSgvivlvgSHNSPSPKGVGYAKNQ 78

                          90       100
                  ....*....|....*....|....*.
gi 1737379514  79 AFSLASGDYITMLDSDDRLKPGSIRD 104
Cdd:cd06913    79 AIAQSSGRYLCFLDSDDVMMPQRIRL 104
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 5-172 2.35e-10

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: 59.10  E-value: 2.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   5 SIIIAAHNAEDTLHTTLESLhdaIDNAGDDVEVIIFNDSSDDSTQDIIEtwlpAFPNVHSRHVQFRNVGLVR--NSAFSL 82
Cdd:cd06433     1 SIITPTYNQAETLEETIDSV---LSQTYPNIEYIVIDGGSTDGTVDIIK----KYEDKITYWISEPDKGIYDamNKGIAL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514  83 ASGDYITMLDSDDRLKPGS-IRDAVAFLKTERPDMLLTRLLEIRDIKKITPNWQGFSPvalsqreaIKRFLLHKDFQAHl 161
Cdd:cd06433    74 ATGDIIGFLNSDDTLLPGAlLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPF--------LDKFLLYGMPICH- 144

                         170
                  ....*....|...
gi 1737379514 162 igQ--FIHRKLYE 172
Cdd:cd06433   145 --QatFFRRSLFE 155
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 4-119 3.34e-09

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 55.67  E-value: 3.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   4 LSIIIAAHNA-EDTLHTTLESLhdaIDNAGDDVEVIIFNDssdDSTQDIIETWLPAFPNVHSR-HVQFR--NVGLVR--N 77
Cdd:cd04184     3 ISIVMPVYNTpEKYLREAIESV---RAQTYPNWELCIADD---ASTDPEVKRVLKKYAAQDPRiKVVFReeNGGISAatN 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1737379514  78 SAFSLASGDYITMLDSDDRLKPGSIRD-AVAFLKTERPDMLLT 119
Cdd:cd04184    77 SALELATGEFVALLDHDDELAPHALYEvVKALNEHPDADLIYS 119
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-115 1.18e-08

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: 53.33  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   6 IIIAAHNAEDTLHTTLESLhdaIDNAGDDVEVIIFNDSSDDSTQDIIETwlpAFPNVhSRHVQFRNVGLVR--NSAFSLA 83
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSL---LAQTYPDFEVIVVDNASTDGSVELLRE---LFPEV-RLIRNGENLGFGAgnNQGIREA 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1737379514  84 SGDYITMLDSDDRLKPGSIRDAVAFLKtERPD 115
Cdd:cd04186    74 KGDYVLLLNPDTVVEPGALLELLDAAE-QDPD 104
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-121 1.79e-08

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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 53.79  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   5 SIIIAAHNAEDTLHTTLESLhdaIDNAGDDVEVIIFNDSSDDSTQDIIETWLPAFPNVHSRHVQFRNVGLVRN--SAFSL 82
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSI---LAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGKNLGVARNfeSLLQA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1737379514  83 ASGDYITMLDSDDRLKPGSIRDAV-AFLKTERPDMLLTRL 121
Cdd:cd04196    78 ADGDYVFFCDQDDIWLPDKLERLLkAFLKDDKPLLVYSDL 117
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 6-110 3.77e-07

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 49.50  E-value: 3.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   6 IIIAAHNAEDTLHTTLESLhdaiDNAGD-DVEVIIFNDSSDDSTQDIIETWLPAFPnVHSRHVQFRNVGL----VRNSAF 80
Cdd:cd06420     1 LIITTYNRPEALELVLKSV----LNQSIlPFEVIIADDGSTEETKELIEEFKSQFP-IPIKHVWQEDEGFrkakIRNKAI 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 1737379514  81 SLASGDYITMLDSDDRLKPGSIRDAVAFLK 110
Cdd:cd06420    76 AAAKGDYLIFIDGDCIPHPDFIADHIELAE 105
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 6-116 5.68e-07

DPG_synthase is involved in protein N-linked glycosylation; 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.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 49.10  E-value: 5.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   6 IIIAAHNAEDTLHTTLESLHDAID-NAGDDVEVIIFNDSSDDSTQDIIETWLPAFPNVhSRHVQF-RNVG---LVRNsAF 80
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEeRPSFSYEIIVVDDGSKDGTAEVARKLARKNPAL-IRVLTLpKNRGkggAVRA-GM 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1737379514  81 SLASGDYITMLDSDDRLKPGSIRDAVAFLKTERPDM 116
Cdd:cd04188    79 LAARGDYILFADADLATPFEELEKLEEALKTSGYDI 114
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 4-185 2.58e-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: 47.57  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   4 LSIIIAAHNAEDTLHTTLESLHDAidnAGDDVEVIIFNDSSDDSTQDIIE----TWLPAFPNvhsRHVQFrNVGlvrnsA 79
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRL---NPLPLEIIVVDGGSTDGTVAIARsagvVVISSPKG---RARQM-NAG-----A 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514  80 fSLASGDYITMLDSDDRLKPGSIRD-----------AVAF-LKTERPDmLLTRLLEIRdikkitPNWQgfspvalsqreA 147
Cdd:cd02522    69 -AAARGDWLLFLHADTRLPPDWDAAiietlradgavAGAFrLRFDDPG-PRLRLLELG------ANLR-----------S 129

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1737379514 148 IKRFLLHKDfQahliGQFIHRKLYES----NPIPSMvcyEDF 185
Cdd:cd02522   130 RLFGLPYGD-Q----GLFIRRELFEElggfPELPLM---EDV 163
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 6-94 2.34e-05

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; 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. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 44.45  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   6 IIIAAHNAEDTLHTTLESLHDAIDNAgdDVEVIIFNDSSDDSTQDIIETWLPAFPNVHSRHvqfRNVGLVRNSA----FS 81
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGI--DYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIV---RPGKRGLGSAyiegFK 75

                          90
                  ....*....|...
gi 1737379514  82 LASGDYITMLDSD 94
Cdd:cd06442    76 AARGDVIVVMDAD 88
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 3-94 5.31e-05

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 43.99  E-value: 5.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   3 FLSIIIAAHNAEDTLHTTLESLHDAIDNAGDD-----VEVIIFNDSSDDSTQDIIETWlpaFPNVHSRHVQFRNVGLVRN 77
Cdd:PTZ00260   71 DLSIVIPAYNEEDRLPKMLKETIKYLESRSRKdpkfkYEIIIVNDGSKDKTLKVAKDF---WRQNINPNIDIRLLSLLRN 147

                          90       100
                  ....*....|....*....|....*
gi 1737379514  78 --------SAFSLASGDYITMLDSD 94
Cdd:PTZ00260  148 kgkggavrIGMLASRGKYILMVDAD 172
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 5-115 2.71e-04

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 41.61  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   5 SIIIAAHNAEDTLHTTLESLHDAIDNAgDDVEVIIFNDSSDDSTQDIIETWLPAFPNVH----SRHvqfRNVGLvrNSAF 80
Cdd:PLN02726   12 SIIVPTYNERLNIALIVYLIFKALQDV-KDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRillrPRP---GKLGL--GTAY 85

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1737379514  81 S----LASGDYITMLDSDDRLKPGSIRDAVAFLKTERPD 115
Cdd:PLN02726   86 IhglkHASGDFVVIMDADLSHHPKYLPSFIKKQRETGAD 124
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 4-107 7.51e-03

undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 37.41  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737379514   4 LSIIIAAHNAEDTLHTTLESLHDAIDNAGDDVEVIIFNDSSDDSTQDIIETWLPAfPNVHSRHVQF-RNVGlvRNSA--- 79
Cdd:PRK10714    8 VSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQA-PDSHIVAILLnRNYG--QHSAima 84

                          90       100
                  ....*....|....*....|....*....
gi 1737379514  80 -FSLASGDYITMLDSDDRLKPGSIRDAVA 107
Cdd:PRK10714   85 gFSHVTGDLIITLDADLQNPPEEIPRLVA 113
 
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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