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Conserved domains on  [gi|2169866321|ref|WP_232774719|]
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MULTISPECIES: glycosyltransferase family 2 protein [Brevibacillus]

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

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  9445404|12691742
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 ...
 6-196 1.20e-54

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: 179.41  E-value: 1.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321   6 LSLCMIVKDEADQIEACLSSVHMVADEIIVIDTGSTDGTQDICRKYGAKVLEIPWENsFAKARNAGLEVAKGEWILWLDA 85
Cdd:cd02511     2 LSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRWWDG-FGAQRNFALELATNDWVLSLDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  86 DEIVQEEKPGVLRQAISASKSDAFFMKMI-HYTGsqkeQASRHSAYR-SGQVRLFRNKKGFRFVRDIHEILQWPTTASRd 163
Cdd:cd02511    81 DERLTPELADEILALLATDDYDGYYVPRRnFFLG----RWIRHGGWYpDRQLRLFRRGKARFEDGRVHEQVVVDGGVGI- 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2169866321 164 iaipLLPVHIHHLGYMDDAvQRKQKALRNLRLL 196
Cdd:cd02511   156 ----VLKGDILHYGYKSLE-EFLEKHNRYSSLE 183
Spy super family cl27809
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 193-309 1.41e-06

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG3914:

Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 49.99  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321 193 LRLLRHERKKSKQDPWCDYHLANEFFRAKQFEYAFTLVNQAMKgflttQKPPPSICYKLKFDILFQHGSMRGAWPGIARA 272
Cdd:COG3914    98 LALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALA-----LNPDFAEAYLNLGEALRRLGRLEEAIAALRRA 172

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2169866321 273 IQIYPNYVDLHFYKGVFLMEHGLYAEAVKAFEYCLEI 309
Cdd:COG3914   173 LELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALEL 209
 
Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 6-196 1.20e-54

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: 179.41  E-value: 1.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321   6 LSLCMIVKDEADQIEACLSSVHMVADEIIVIDTGSTDGTQDICRKYGAKVLEIPWENsFAKARNAGLEVAKGEWILWLDA 85
Cdd:cd02511     2 LSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRWWDG-FGAQRNFALELATNDWVLSLDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  86 DEIVQEEKPGVLRQAISASKSDAFFMKMI-HYTGsqkeQASRHSAYR-SGQVRLFRNKKGFRFVRDIHEILQWPTTASRd 163
Cdd:cd02511    81 DERLTPELADEILALLATDDYDGYYVPRRnFFLG----RWIRHGGWYpDRQLRLFRRGKARFEDGRVHEQVVVDGGVGI- 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2169866321 164 iaipLLPVHIHHLGYMDDAvQRKQKALRNLRLL 196
Cdd:cd02511   156 ----VLKGDILHYGYKSLE-EFLEKHNRYSSLE 183
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 3-198 2.64e-26

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 104.40  E-value: 2.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321   3 PPLLSLCMIVKDEADQIEACLSSVHMVAD---EIIVIDTGSTDGTQDICRKYGA-----KVLEIPWENSFAKARNAGLEV 74
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYpdfEIIVVDDGSTDGTAEILRELAAkdpriRVIRLERNRGKGAARNAGLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  75 AKGEWILWLDADEIVQEEKPGVLRQAISASKSDAFFMKMIHYTGSQ--KEQASRHSAYRSGQVRLFRNKKGFRFV-RDIH 151
Cdd:COG0463    81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESdlRRLGSRLFNLVRLLTNLPDSTSGFRLFrREVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2169866321 152 EILQWPTTASRDIAIPLLPVHIHHLGYMDDAVQRKQKALRNLRLLRH 198
Cdd:COG0463   161 EELGFDEGFLEDTELLRALRHGFRIAEVPVRYRAGESKLNLRDLLRL 207
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 7-151 1.27e-20

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: 87.45  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321   7 SLCMIVKDEADQIEACLSSV---HMVADEIIVIDTGSTDGTQDICRKY-----GAKVLEIPWENSFAKARNAGLEVAKGE 78
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLlnqTYPNFEIIVVDDGSTDGTVEIAEEYakkdpRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2169866321  79 WILWLDADEIVQEEKPGVLRQAISASKSDAFFMKMIHYTGSQKEQASRHSAYRSGQVRLFRNKKGFRFVRDIH 151
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLI 153
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 2-89 2.65e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 57.75  E-value: 2.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321   2 SPPLLSLCMIVKDEADQIEACLSSVH---MVADEIIVIDTGSTDGTQDICRKYGAK---VLEIPWENSFAK-ARNAGLEV 74
Cdd:PRK10073    4 STPKLSIIIPLYNAGKDFRAFMESLIaqtWTALEIIIVNDGSTDNSVEIAKHYAENyphVRLLHQANAGVSvARNTGLAV 83

                          90
                  ....*....|....*
gi 2169866321  75 AKGEWILWLDADEIV 89
Cdd:PRK10073   84 ATGKYVAFPDADDVV 98
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 193-309 1.41e-06

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 49.99  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321 193 LRLLRHERKKSKQDPWCDYHLANEFFRAKQFEYAFTLVNQAMKgflttQKPPPSICYKLKFDILFQHGSMRGAWPGIARA 272
Cdd:COG3914    98 LALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALA-----LNPDFAEAYLNLGEALRRLGRLEEAIAALRRA 172

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2169866321 273 IQIYPNYVDLHFYKGVFLMEHGLYAEAVKAFEYCLEI 309
Cdd:COG3914   173 LELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALEL 209
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
32-88 2.48e-05

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 45.55  E-value: 2.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2169866321  32 EIIVIDTGSTDGTQDICRKYGAKvleipWENSF------------AKARNAGLEVAKGEWILWLDADEI 88
Cdd:NF038302   35 EIIVVDNNSTDNTAQVVQEYQKN-----WPSPYplrycfepqqgaAFARQRAIQEAKGELIGFLDDDNL 98
 
Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 6-196 1.20e-54

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: 179.41  E-value: 1.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321   6 LSLCMIVKDEADQIEACLSSVHMVADEIIVIDTGSTDGTQDICRKYGAKVLEIPWENsFAKARNAGLEVAKGEWILWLDA 85
Cdd:cd02511     2 LSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRWWDG-FGAQRNFALELATNDWVLSLDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  86 DEIVQEEKPGVLRQAISASKSDAFFMKMI-HYTGsqkeQASRHSAYR-SGQVRLFRNKKGFRFVRDIHEILQWPTTASRd 163
Cdd:cd02511    81 DERLTPELADEILALLATDDYDGYYVPRRnFFLG----RWIRHGGWYpDRQLRLFRRGKARFEDGRVHEQVVVDGGVGI- 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2169866321 164 iaipLLPVHIHHLGYMDDAvQRKQKALRNLRLL 196
Cdd:cd02511   156 ----VLKGDILHYGYKSLE-EFLEKHNRYSSLE 183
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 3-198 2.64e-26

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 104.40  E-value: 2.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321   3 PPLLSLCMIVKDEADQIEACLSSVHMVAD---EIIVIDTGSTDGTQDICRKYGA-----KVLEIPWENSFAKARNAGLEV 74
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYpdfEIIVVDDGSTDGTAEILRELAAkdpriRVIRLERNRGKGAARNAGLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  75 AKGEWILWLDADEIVQEEKPGVLRQAISASKSDAFFMKMIHYTGSQ--KEQASRHSAYRSGQVRLFRNKKGFRFV-RDIH 151
Cdd:COG0463    81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESdlRRLGSRLFNLVRLLTNLPDSTSGFRLFrREVL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2169866321 152 EILQWPTTASRDIAIPLLPVHIHHLGYMDDAVQRKQKALRNLRLLRH 198
Cdd:COG0463   161 EELGFDEGFLEDTELLRALRHGFRIAEVPVRYRAGESKLNLRDLLRL 207
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 7-151 1.27e-20

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: 87.45  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321   7 SLCMIVKDEADQIEACLSSV---HMVADEIIVIDTGSTDGTQDICRKY-----GAKVLEIPWENSFAKARNAGLEVAKGE 78
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLlnqTYPNFEIIVVDDGSTDGTVEIAEEYakkdpRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2169866321  79 WILWLDADEIVQEEKPGVLRQAISASKSDAFFMKMIHYTGSQKEQASRHSAYRSGQVRLFRNKKGFRFVRDIH 151
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLI 153
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
2-104 4.62e-19

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 84.27  E-value: 4.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321   2 SPPLLSLCMIVKDEADQIEACLSSVH---MVADEIIVIDTGSTDGTQDICRKY---GAKVLEIPWENSFAKARNAGLEVA 75
Cdd:COG1216     1 MRPKVSVVIPTYNRPELLRRCLESLLaqtYPPFEVIVVDNGSTDGTAELLAALafpRVRVIRNPENLGFAAARNLGLRAA 80

                          90       100
                  ....*....|....*....|....*....
gi 2169866321  76 KGEWILWLDADEIVQeekPGVLRQAISAS 104
Cdd:COG1216    81 GGDYLLFLDDDTVVE---PDWLERLLAAA 106
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 4-103 8.79e-18

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: 82.87  E-value: 8.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321   4 PLLSLCMIVKDEADQIEACLSSVH-----MVADEIIVIDTGSTDGTQDICRKYGA-----KVLEIPWENSFAKARNAGLE 73
Cdd:COG1215    29 PRVSVIIPAYNEEAVIEETLRSLLaqdypKEKLEVIVVDDGSTDETAEIARELAAeyprvRVIERPENGGKAAALNAGLK 108

                          90       100       110
                  ....*....|....*....|....*....|
gi 2169866321  74 VAKGEWILWLDADEIVqeeKPGVLRQAISA 103
Cdd:COG1215   109 AARGDIVVFLDADTVL---DPDWLRRLVAA 135
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 10-93 1.87e-17

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: 78.70  E-value: 1.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  10 MIVKDEADQIEACLSSVH---MVADEIIVIDTGSTDGTQDICRKYGAK----VLEIPWENS-FAKARNAGLEVAKGEWIL 81
Cdd:cd00761     3 IPAYNEEPYLERCLESLLaqtYPNFEVIVVDDGSTDGTLEILEEYAKKdprvIRVINEENQgLAAARNAGLKAARGEYIL 82

                          90
                  ....*....|..
gi 2169866321  82 WLDADEIVQEEK 93
Cdd:cd00761    83 FLDADDLLLPDW 94
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 13-107 1.80e-14

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: 70.72  E-value: 1.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  13 KDEADQIEACLSSvhMVA-----DEIIVIDTGSTDGTQDICRKYGA-----KVLEIPWENSF-AKARNAGLEVAKGEWIL 81
Cdd:cd06423     6 YNEEAVIERTIES--LLAldypkLEVIVVDDGSTDDTLEILEELAAlyirrVLVVRDKENGGkAGALNAGLRHAKGDIVV 83

                          90       100
                  ....*....|....*....|....*.
gi 2169866321  82 WLDADEIVQeekPGVLRQAISASKSD 107
Cdd:cd06423    84 VLDADTILE---PDALKRLVVPFFAD 106
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 7-86 1.53e-13

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: 69.57  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321   7 SLCMIVKDEADQIEACLSSV-----HMVADEIIVIDTGSTDGTQDICRKYGAKVLEIPWEN----SFAKARNAGLEVAKG 77
Cdd:cd02525     3 SIIIPVRNEEKYIEELLESLlnqsyPKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDnpkrIQSAGLNIGIRNSRG 82


                  ....*....
gi 2169866321  78 EWILWLDAD 86
Cdd:cd02525    83 DIIIRVDAH 91
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 10-107 2.07e-12

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: 64.50  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  10 MIVKDEADQIEACLSSV---HMVADEIIVIDTGSTDGTQDICRKYGAKVLEIPWENS--FAKARNAGLEVAKGEWILWLD 84
Cdd:cd04186     3 IVNYNSLEYLKACLDSLlaqTYPDFEVIVVDNASTDGSVELLRELFPEVRLIRNGENlgFGAGNNQGIREAKGDYVLLLN 82

                          90       100
                  ....*....|....*....|...
gi 2169866321  85 ADEIVQeekPGVLRQAISASKSD 107
Cdd:cd04186    83 PDTVVE---PGALLELLDAAEQD 102
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 15-86 3.31e-11

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: 61.44  E-value: 3.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  15 EADQIEACLSSVHMVA-----DEIIVIDTGSTDGTQDICRKYGAKVleiPWENSFAKARN--------AGLEVAKGEWIL 81
Cdd:cd04179     8 EEENIPELVERLLAVLeegydYEIIVVDDGSTDGTAEIARELAARV---PRVRVIRLSRNfgkgaavrAGFKAARGDIVV 84


                  ....*
gi 2169866321  82 WLDAD 86
Cdd:cd04179    85 TMDAD 89
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 14-108 8.12e-11

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: 61.05  E-value: 8.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  14 DEADQIEACLSSV---HMVADEIIVIDTGSTDGTQDICRKYGAKVLEIPwensfaKAR----NAGLEVAKGEWILWLDAD 86
Cdd:cd02522     9 NEAENLPRLLASLrrlNPLPLEIIVVDGGSTDGTVAIARSAGVVVISSP------KGRarqmNAGAAAARGDWLLFLHAD 82

                          90       100
                  ....*....|....*....|..
gi 2169866321  87 EIVqeeKPGVLRQAISASKSDA 108
Cdd:cd02522    83 TRL---PPDWDAAIIETLRADG 101
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 16-86 8.82e-11

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: 60.64  E-value: 8.82e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2169866321  16 ADQIEACLSSVHM---VADEIIVIDTGSTDGTQDICRKYGAKVLEIPWENSF--AKARNAGLEVAKGEWILWLDAD 86
Cdd:cd06433    10 AETLEETIDSVLSqtyPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKgiYDAMNKGIALATGDIIGFLNSD 85
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 2-89 2.65e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 57.75  E-value: 2.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321   2 SPPLLSLCMIVKDEADQIEACLSSVH---MVADEIIVIDTGSTDGTQDICRKYGAK---VLEIPWENSFAK-ARNAGLEV 74
Cdd:PRK10073    4 STPKLSIIIPLYNAGKDFRAFMESLIaqtWTALEIIIVNDGSTDNSVEIAKHYAENyphVRLLHQANAGVSvARNTGLAV 83

                          90
                  ....*....|....*
gi 2169866321  75 AKGEWILWLDADEIV 89
Cdd:PRK10073   84 ATGKYVAFPDADDVV 98
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 15-86 1.03e-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: 51.80  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  15 EADQIEACLSSVHMVAD-------EIIVIDTGSTDGTQDICRKYGAK------VLEIPwENSfAKAR--NAGLEVAKGEW 79
Cdd:cd04188     8 EEKRLPPTLEEAVEYLEerpsfsyEIIVVDDGSKDGTAEVARKLARKnpalirVLTLP-KNR-GKGGavRAGMLAARGDY 85


                  ....*..
gi 2169866321  80 ILWLDAD 86
Cdd:cd04188    86 ILFADAD 92
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 17-86 4.62e-07

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: 50.22  E-value: 4.62e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2169866321  17 DQIEACLSSVHMvadEIIVIDTGSTDGTQDICRKYGAKVLEI-----PWENSFAKARNAGLEVAKGEWILWLDAD 86
Cdd:cd06442    17 ERLDAALKGIDY---EIIVVDDNSPDGTAEIVRELAKEYPRVrlivrPGKRGLGSAYIEGFKAARGDVIVVMDAD 88
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 12-86 6.28e-07

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: 49.01  E-value: 6.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  12 VKDEADQIEACLSSVHMVAD------EIIVIDTGSTDGTQDICRKYGAKvleipweNSFAK----ARN--------AGLE 73
Cdd:cd04187     5 VYNEEENLPELYERLKAVLEslgydyEIIFVDDGSTDRTLEILRELAAR-------DPRVKvirlSRNfgqqaallAGLD 77

                          90
                  ....*....|...
gi 2169866321  74 VAKGEWILWLDAD 86
Cdd:cd04187    78 HARGDAVITMDAD 90
Glyco_tranf_2_4 pfam13704
Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative ...
 13-89 1.08e-06

Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative glucosyltransferases,


Pssm-ID: 433416 [Multi-domain]  Cd Length: 97  Bit Score: 46.47  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  13 KDEADQIEACLSsvH---MVADEIIVIDTGSTDGTQDICRKYGAKVLeIPWENSFAKAR------NAGL-EVAKGEWILW 82
Cdd:pfam13704   1 RNEADILPQWLA--HhlaLGFDHIYVYDNGSDDGTAEILARLPDVSI-LRSDLSYKDARfqvdwrNALLaRYAEADWVLV 77


                  ....*..
gi 2169866321  83 LDADEIV 89
Cdd:pfam13704  78 VDADEFL 84
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 193-309 1.41e-06

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 49.99  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321 193 LRLLRHERKKSKQDPWCDYHLANEFFRAKQFEYAFTLVNQAMKgflttQKPPPSICYKLKFDILFQHGSMRGAWPGIARA 272
Cdd:COG3914    98 LALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALA-----LNPDFAEAYLNLGEALRRLGRLEEAIAALRRA 172

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2169866321 273 IQIYPNYVDLHFYKGVFLMEHGLYAEAVKAFEYCLEI 309
Cdd:COG3914   173 LELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALEL 209
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 12-92 2.10e-06

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: 48.05  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  12 VKDEADQIEACLSSV--------HMvadEIIVIDTGSTDGTQDICRKYGAK------VLEIPW-ENSF-AKARNAGLEVA 75
Cdd:cd04192     5 ARNEAENLPRLLQSLsaldypkeKF---EVILVDDHSTDGTVQILEFAAAKpnfqlkILNNSRvSISGkKNALTTAIKAA 81

                          90
                  ....*....|....*..
gi 2169866321  76 KGEWILWLDADEIVQEE 92
Cdd:cd04192    82 KGDWIVTTDADCVVPSN 98
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 7-86 3.38e-06

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 48.38  E-value: 3.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321   7 SLCMIVKDEADQIEACLSSVH---MVA--DEIIVIDTGSTDGTQDICRKYGAKVL-------EIP---------Wensfa 65
Cdd:PRK13915   34 SVVLPALNEEETVGKVVDSIRpllMEPlvDELIVIDSGSTDATAERAAAAGARVVsreeilpELPprpgkgealW----- 108

                          90       100
                  ....*....|....*....|.
gi 2169866321  66 karnAGLEVAKGEWILWLDAD 86
Cdd:PRK13915  109 ----RSLAATTGDIVVFVDAD 125
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 2-101 3.41e-06

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: 47.96  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321   2 SPPLLSLCMIVKDEADQIEACLSSVHMV---AD--EIIVIDTGSTDGTQDICRKYGA---KVLEIPwENS-FAKARNAGL 72
Cdd:cd06439    27 YLPTVTIIIPAYNEEAVIEAKLENLLALdypRDrlEIIVVSDGSTDGTAEIAREYADkgvKLLRFP-ERRgKAAALNRAL 105

                          90       100
                  ....*....|....*....|....*....
gi 2169866321  73 EVAKGEWILWLDADEIVqeeKPGVLRQAI 101
Cdd:cd06439   106 ALATGEIVVFTDANALL---DPDALRLLV 131
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 211-343 5.67e-06

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 45.57  E-value: 5.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321 211 YHLANEFFRAKQFEYAFTLVNQAMKgfLTTQKPPPsicYKLKFDILFQHGSMRGAWPGIARAIQIYPNYVDLHFYKGVFL 290
Cdd:COG4783     8 YALAQALLLAGDYDEAEALLEKALE--LDPDNPEA---FALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLAL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2169866321 291 MEHGLYAEAVKAFEYCLEIGDNQWEhfseqgmgsfyAFHFLGRCMERMGKTHE 343
Cdd:COG4783    83 LKAGDYDEALALLEKALKLDPEHPE-----------AYLRLARAYRALGRPDE 124
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 20-90 8.11e-06

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: 45.65  E-value: 8.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  20 EACLSSV---HMVADEIIVIDTGSTDGTQDICRKYGAKVlEIP----W--ENSF--AKARNAGLEVAKGEWILWLDADEI 88
Cdd:cd06420    13 ELVLKSVlnqSILPFEVIIADDGSTEETKELIEEFKSQF-PIPikhvWqeDEGFrkAKIRNKAIAAAKGDYLIFIDGDCI 91


                  ..
gi 2169866321  89 VQ 90
Cdd:cd06420    92 PH 93
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 172-345 1.04e-05

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 47.30  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321 172 HIHHLGYMDDAVQRKQKALRNLRLLRHERKKSKQDPWCDYHLANEFFRAKQFEYAFTLVNQAMKGFLTTQKPPPSICYKL 251
Cdd:COG3914     2 AAAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321 252 KFDILFQHGSMR--GAWPGIARAIQIYPNYVDLHFYKGVFLMEHGLYAEAVKAFEYCLEIGDNQWEhfseqgmgsfyAFH 329
Cdd:COG3914    82 ELAALLLQALGRyeEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAE-----------AYL 150

                         170
                  ....*....|....*.
gi 2169866321 330 FLGRCMERMGKTHESL 345
Cdd:COG3914   151 NLGEALRRLGRLEEAI 166
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 32-86 1.12e-05

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 46.23  E-value: 1.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2169866321  32 EIIVIDTGSTDGTQDICRK----YGAKVLEI---PWENSFAKARNAGLEVAKGEWILWLDAD 86
Cdd:PLN02726   42 EIIVVDDGSPDGTQDVVKQlqkvYGEDRILLrprPGKLGLGTAYIHGLKHASGDFVVIMDAD 103
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
174-347 1.33e-05

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 46.15  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321 174 HHLGYMDDAVQRKQKALRnlrLLRHERKKSKQDPWCDYHLANEFFRAKQFEYAFTLVNQAMKgflttQKPPPSICYKLKF 253
Cdd:COG0457    12 NNLGLAYRRLGRYEEAIE---DYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALE-----LDPDDAEALNNLG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321 254 DILFQHGSMRGAWPGIARAIQIYPNYVDLHFYKGVFLMEHGLYAEAVKAFEYCLEIGDNQWEhfseqgmgsfyAFHFLGR 333
Cdd:COG0457    84 LALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDAD-----------ALYNLGI 152

                         170
                  ....*....|....
gi 2169866321 334 CMERMGKTHESLVY 347
Cdd:COG0457   153 ALEKLGRYEEALEL 166
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
32-88 2.48e-05

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 45.55  E-value: 2.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2169866321  32 EIIVIDTGSTDGTQDICRKYGAKvleipWENSF------------AKARNAGLEVAKGEWILWLDADEI 88
Cdd:NF038302   35 EIIVVDNNSTDNTAQVVQEYQKN-----WPSPYplrycfepqqgaAFARQRAIQEAKGELIGFLDDDNL 98
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 4-88 2.62e-05

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: 44.50  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321   4 PLLSLCMIV-KDEADQIEACLSSVHM-VAD--EIIVIDTGSTD-GTQDICRKYGA-----KVLEIPWENSFAKARNAGLE 73
Cdd:cd04184     1 PLISIVMPVyNTPEKYLREAIESVRAqTYPnwELCIADDASTDpEVKRVLKKYAAqdpriKVVFREENGGISAATNSALE 80

                          90
                  ....*....|....*
gi 2169866321  74 VAKGEWILWLDADEI 88
Cdd:cd04184    81 LATGEFVALLDHDDE 95
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 3-107 4.50e-05

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: 44.28  E-value: 4.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321   3 PPLLSLCMIVKDEADQIEACLSSV---HMVADEIIVIDTGSTDGTQDICRKYGAK----------VLEIPWENSFAKARN 69
Cdd:pfam13641   1 PPDVSVVVPAFNEDSVLGRVLEAIlaqPYPPVEVVVVVNPSDAETLDVAEEIAARfpdvrlrvirNARLLGPTGKSRGLN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2169866321  70 AGLEVAKGEWILWLDADEIVQeekPGVLRQAISASKSD 107
Cdd:pfam13641  81 HGFRAVKSDLVVLHDDDSVLH---PGTLKKYVQYFDSP 115
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 12-88 8.52e-05

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which 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.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 43.07  E-value: 8.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  12 VKDEADQIEACLSSVH---MVADEIIVIDTGSTdgTQDI-------CRKYGAKVLEIPWENSFAKARNAGLEVAKGEWIL 81
Cdd:cd04195     8 IKEKPEFLREALESILkqtLPPDEVVLVKDGPV--TQSLnevleefKRKLPLKVVPLEKNRGLGKALNEGLKHCTYDWVA 85


                  ....*..
gi 2169866321  82 WLDADEI 88
Cdd:cd04195    86 RMDTDDI 92
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 174-347 1.74e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 42.79  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321 174 HHLGYMDDAVQRKQKALRNLRLLRherKKSKQDPWCDYHLANEFFRAKQFEYAFTLVNQAMKgflttQKPPPSICYKLKF 253
Cdd:COG2956    80 LELAQDYLKAGLLDRAEELLEKLL---ELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLK-----LGPENAHAYCELA 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321 254 DILFQHGSMRGAWPGIARAIQIYPNYVDLHFYKGVFLMEHGLYAEAVKAFEYCLEIGDNqwehfseqgmgSFYAFHFLGR 333
Cdd:COG2956   152 ELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPD-----------YLPALPRLAE 220

                         170
                  ....*....|....
gi 2169866321 334 CMERMGKTHESLVY 347
Cdd:COG2956   221 LYEKLGDPEEALEL 234
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 254-309 1.91e-04

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 40.76  E-value: 1.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2169866321 254 DILFQHGSMRGAWPGIARAIQIYPNYVDLHFYKGVFLMEHGLYAEAVKAFEYCLEI 309
Cdd:COG4235    59 EALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLAL 114
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 13-181 2.13e-04

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 42.27  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  13 KDEADQIEACLSSVHMVADEIIVIDTGStDGTQDIC-RKYGAKVLEIP-WENS-FAKARNAGLEVAKG---EWILWLDAD 86
Cdd:cd02526     7 NPDLSKLKELLAALAEQVDKVVVVDNSS-GNDIELRlRLNSEKIELIHlGENLgIAKALNIGIKAALEngaDYVLLFDQD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321  87 EIVqeekpgvlrqaisaskSDAFFMKMIHYtGSQKEQASRHSAY--RSGQVRLFRNKKGFRFVRDIHEILQWPTTASRDI 164
Cdd:cd02526    86 SVP----------------PPDMVEKLLAY-KILSDKNSNIGAVgpRIIDRRTGENSPGVRKSGYKLRIQKEGEEGLKEV 148

                         170       180
                  ....*....|....*....|...
gi 2169866321 165 AIP-----LLPVH-IHHLGYMDD 181
Cdd:cd02526   149 DFLitsgsLISLEaLEKVGGFDE 171
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 249-343 3.38e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 40.71  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321 249 YKLKFDILFQHGSMRGAWPGIARAIQIYPNYVDLHFYKGVFLMEHGLYAEAVKAFEYCLEIGDNQWEhfseqgmgsfyAF 328
Cdd:COG5010    57 ESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPN-----------AY 125

                          90
                  ....*....|....*
gi 2169866321 329 HFLGRCMERMGKTHE 343
Cdd:COG5010   126 SNLAALLLSLGQDDE 140
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 271-345 4.50e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 42.29  E-value: 4.50e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2169866321 271 RAIQIYPNYVDLHFYKGVFLMEHGLYAEAVKAFEYCLEIGDNQWEHFSEqgmgsfyafhfLGRCMERMGKTHESL 345
Cdd:COG3914   137 RALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNN-----------LGNALQDLGRLEEAI 200
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
273-345 9.22e-04

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 40.38  E-value: 9.22e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2169866321 273 IQIYPNYVDLHFYKGVFLMEHGLYAEAVKAFEYCLEIGDNQWEhfseqgmgsfyAFHFLGRCMERMGKTHESL 345
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAE-----------ALYNLGLAYLRLGRYEEAL 62
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
271-343 1.24e-03

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 39.90  E-value: 1.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2169866321 271 RAIQIYPNYVDLHFYKGVFLMEHGLYAEAVKAFEYCLEIGDNqwehfseqgmgSFYAFHFLGRCMERMGKTHE 343
Cdd:COG4785    98 QALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPD-----------YAYAYLNRGIALYYLGRYEL 159
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 176-309 3.85e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 37.48  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321 176 LGYMDDAVQRKQKALRnlrLLRHERKKSKQDPWCDYHLANEFFRAKQFEYAFTLVNQAMKgflttQKPPPSICYKLKFDI 255
Cdd:COG4783    10 LAQALLLAGDYDEAEA---LLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALE-----LDPDEPEARLNLGLA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2169866321 256 LFQHGSMRGAWPGIARAIQIYPNYVDLHFYKGVFLMEHGLYAEAVKAFEYCLEI 309
Cdd:COG4783    82 LLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALEL 135
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 31-93 4.30e-03

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: 38.00  E-value: 4.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2169866321  31 DEIIVIDTGSTDGTQDICRKYGAK-----VLEIPWEN-SFAKARNAGLEVAKGEWILWLDADEIVQEEK 93
Cdd:cd04196    28 DELIISDDGSTDGTVEIIKEYIDKdpfiiILIRNGKNlGVARNFESLLQAADGDYVFFCDQDDIWLPDK 96
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
271-347 4.91e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 35.92  E-value: 4.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2169866321 271 RAIQIYPNYVDLHFYKGVFLMEHGLYAEAvKAFEYCLEIGDNQWEhfseqgmgsfyAFHFLGRCMERMGKTHESLVY 347
Cdd:COG3063    17 KALELDPDNADALNNLGLLLLEQGRYDEA-IALEKALKLDPNNAE-----------ALLNLAELLLELGDYDEALAY 81
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 187-317 5.37e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 38.17  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2169866321 187 QKALRNLRLLRherKKSKQDPWCDYHLANEFFRAKQFEYAFTLVNQAMKgflTTQKPPPSicYKLKFDILFQHGSMRGAW 266
Cdd:COG2956   127 EKAIEVLERLL---KLGPENAHAYCELAELYLEQGDYDEAIEALEKALK---LDPDCARA--LLLLAELYLEQGDYEEAI 198

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2169866321 267 PGIARAIQIYPNYVDLHFYKGVFLMEHGLYAEAVKAFEYCLEIGDNQWEHF 317
Cdd:COG2956   199 AALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLL 249
 
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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