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Conserved domains on  [gi|497584324|ref|WP_009898508|]
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glycosyltransferase family 2 protein [Clostridioides difficile]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10118426)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 3-225 1.73e-45

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: 155.14  E-value: 1.73e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324   3 TISLCMIVKNEEEVIGRCLECVKDIVDEIIIVDTGSTDSTKEIVSKYTDMVYDFEWiDDFSAARNFSFSKASKDYTMWLD 82
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRWW-DGFGAQRNFALELATNDWVLSLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324  83 ADDIILEADREKLLKIKESLDTSIDIVMAKYNVsFDENGNPTLSY--YRERLFKRSSNHKWVDPIHE-VVPLFGEVFYSD 159
Cdd:cd02511   80 ADERLTPELADEILALLATDDYDGYYVPRRNFF-LGRWIRHGGWYpdRQLRLFRRGKARFEDGRVHEqVVVDGGVGIVLK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 160 IAISHK-------KLHRQDplRNLRIFEK-MISEGK------TLEPRHQFYYSRELYYNARYkeaiegftkFLDSSRGWI 225
Cdd:cd02511  159 GDILHYgyksleeFLEKHN--RYSSLEAKdLAAKGKkrsllkGLLLGRPLLAFLKMYILKRG---------FLDGRAGFI 227
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 176-348 7.72e-10

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: 58.97  E-value: 7.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 176 LRIFEKMISegktLEPRHQFYYSR--ELYYNA-RYKEAIEGFTKFLDSSrgwiEDCISACRDLATCYYLINDEKSALYSL 252
Cdd:COG2956   62 IRIHQKLLE----RDPDRAEALLElaQDYLKAgLLDRAEELLEKLLELD----PDDAEALRLLAEIYEQEGDWEKAIEVL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 253 FRSFEFDEPRAEICCDIGKHMFDRQKYKEAIFWYKVALTRDKNDTNggfksndcygyiPSIQLSVCYDRLGESDKAIYYH 332
Cdd:COG2956  134 ERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCAR------------ALLLLAELYLEQGDYEEAIAAL 201

                        170
                 ....*....|....*.
gi 497584324 333 EKTKEIKPNDSAVLHN 348
Cdd:COG2956  202 ERALEQDPDYLPALPR 217
 
Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 3-225 1.73e-45

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: 155.14  E-value: 1.73e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324   3 TISLCMIVKNEEEVIGRCLECVKDIVDEIIIVDTGSTDSTKEIVSKYTDMVYDFEWiDDFSAARNFSFSKASKDYTMWLD 82
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRWW-DGFGAQRNFALELATNDWVLSLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324  83 ADDIILEADREKLLKIKESLDTSIDIVMAKYNVsFDENGNPTLSY--YRERLFKRSSNHKWVDPIHE-VVPLFGEVFYSD 159
Cdd:cd02511   80 ADERLTPELADEILALLATDDYDGYYVPRRNFF-LGRWIRHGGWYpdRQLRLFRRGKARFEDGRVHEqVVVDGGVGIVLK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 160 IAISHK-------KLHRQDplRNLRIFEK-MISEGK------TLEPRHQFYYSRELYYNARYkeaiegftkFLDSSRGWI 225
Cdd:cd02511  159 GDILHYgyksleeFLEKHN--RYSSLEAKdLAAKGKkrsllkGLLLGRPLLAFLKMYILKRG---------FLDGRAGFI 227
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-138 2.67e-22

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 93.23  E-value: 2.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324   1 MITISLCMIVKNEEEVIGRCLECVK---DIVDEIIIVDTGSTDSTKEIVSKYTDMVYDFEWID-----DFSAARNFSFSK 72
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLaqtYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRlernrGKGAARNAGLAA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497584324  73 ASKDYTMWLDADDIILEADREKLLKIKEslDTSIDIVMAKYNVSFDENGNPTLSYYRERLFKRSSN 138
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALE--EGPADLVYGSRLIREGESDLRRLGSRLFNLVRLLTN 144
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-150 7.57e-19

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: 82.44  E-value: 7.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324    5 SLCMIVKNEEEVIGRCLECVKDI---VDEIIIVDTGSTDSTKEIVSKYTDM-----VYDFEWIDDFSAARNFSFSKASKD 76
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQtypNFEIIVVDDGSTDGTVEIAEEYAKKdprvrVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497584324   77 YTMWLDADDIILEADREKLLKIKESLDTsiDIVMAKYNVSFDENGN--PTLSYYRERLFKRSSNHKWVDPIHEVVP 150
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGA--DVVVGSRYVIFGETGEyrRASRITLSRLPFFLGLRLLGLNLPFLIG 154
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 176-348 7.72e-10

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: 58.97  E-value: 7.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 176 LRIFEKMISegktLEPRHQFYYSR--ELYYNA-RYKEAIEGFTKFLDSSrgwiEDCISACRDLATCYYLINDEKSALYSL 252
Cdd:COG2956   62 IRIHQKLLE----RDPDRAEALLElaQDYLKAgLLDRAEELLEKLLELD----PDDAEALRLLAEIYEQEGDWEKAIEVL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 253 FRSFEFDEPRAEICCDIGKHMFDRQKYKEAIFWYKVALTRDKNDTNggfksndcygyiPSIQLSVCYDRLGESDKAIYYH 332
Cdd:COG2956  134 ERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCAR------------ALLLLAELYLEQGDYEEAIAAL 201

                        170
                 ....*....|....*.
gi 497584324 333 EKTKEIKPNDSAVLHN 348
Cdd:COG2956  202 ERALEQDPDYLPALPR 217
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 30-121 3.35e-08

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 54.28  E-value: 3.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324  30 EIIIVDTGSTDSTKEIVSKYTDMVYDFEWIDD----FSAARNFSFSKASKDYTMWLDADDIILEADREKLLKIKESLDts 105
Cdd:PRK10073  37 EIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQanagVSVARNTGLAVATGKYVAFPDADDVVYPTMYETLMTMALEDD-- 114

                         90
                 ....*....|....*.
gi 497584324 106 IDIVMAKYNVSFDENG 121
Cdd:PRK10073 115 LDVAQCNADWCFRDTG 130
 
Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 3-225 1.73e-45

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: 155.14  E-value: 1.73e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324   3 TISLCMIVKNEEEVIGRCLECVKDIVDEIIIVDTGSTDSTKEIVSKYTDMVYDFEWiDDFSAARNFSFSKASKDYTMWLD 82
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRWW-DGFGAQRNFALELATNDWVLSLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324  83 ADDIILEADREKLLKIKESLDTSIDIVMAKYNVsFDENGNPTLSY--YRERLFKRSSNHKWVDPIHE-VVPLFGEVFYSD 159
Cdd:cd02511   80 ADERLTPELADEILALLATDDYDGYYVPRRNFF-LGRWIRHGGWYpdRQLRLFRRGKARFEDGRVHEqVVVDGGVGIVLK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 160 IAISHK-------KLHRQDplRNLRIFEK-MISEGK------TLEPRHQFYYSRELYYNARYkeaiegftkFLDSSRGWI 225
Cdd:cd02511  159 GDILHYgyksleeFLEKHN--RYSSLEAKdLAAKGKkrsllkGLLLGRPLLAFLKMYILKRG---------FLDGRAGFI 227
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-138 2.67e-22

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 93.23  E-value: 2.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324   1 MITISLCMIVKNEEEVIGRCLECVK---DIVDEIIIVDTGSTDSTKEIVSKYTDMVYDFEWID-----DFSAARNFSFSK 72
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLaqtYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRlernrGKGAARNAGLAA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497584324  73 ASKDYTMWLDADDIILEADREKLLKIKEslDTSIDIVMAKYNVSFDENGNPTLSYYRERLFKRSSN 138
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALE--EGPADLVYGSRLIREGESDLRRLGSRLFNLVRLLTN 144
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-150 7.57e-19

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: 82.44  E-value: 7.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324    5 SLCMIVKNEEEVIGRCLECVKDI---VDEIIIVDTGSTDSTKEIVSKYTDM-----VYDFEWIDDFSAARNFSFSKASKD 76
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQtypNFEIIVVDDGSTDGTVEIAEEYAKKdprvrVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497584324   77 YTMWLDADDIILEADREKLLKIKESLDTsiDIVMAKYNVSFDENGN--PTLSYYRERLFKRSSNHKWVDPIHEVVP 150
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGA--DVVVGSRYVIFGETGEyrRASRITLSRLPFFLGLRLLGLNLPFLIG 154
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 8-118 2.11e-14

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


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 69.84  E-value: 2.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324   8 MIVKNEEEVIGRCLECVKDI---VDEIIIVDTGSTDSTKEIVSKYTDM-----VYDFEWIDDFSAARNFSFSKASKDYTM 79
Cdd:cd00761    3 IPAYNEEPYLERCLESLLAQtypNFEVIVVDDGSTDGTLEILEEYAKKdprviRVINEENQGLAAARNAGLKAARGEYIL 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 497584324  80 WLDADDiILEADREKLLKIKESLDTSIDIVMAKYNVSFD 118
Cdd:cd00761   83 FLDADD-LLLPDWLERLVAELLADPEADAVGGPGNLLFR 120
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 1-87 7.51e-12

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: 65.15  E-value: 7.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324   1 MITISLCMIVKNEEEVIGRCLECVKDI-----VDEIIIVDTGSTDSTKEIVSKYTDMVYDFEWIDD-----FSAARNFSF 70
Cdd:COG1215   28 LPRVSVIIPAYNEEAVIEETLRSLLAQdypkeKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERpenggKAAALNAGL 107

                         90
                 ....*....|....*..
gi 497584324  71 SKASKDYTMWLDADDII 87
Cdd:COG1215  108 KAARGDIVVFLDADTVL 124
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 3-109 1.07e-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: 64.18  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324   3 TISLCMIVKNEEEVIGRCLECV------KDIVdEIIIVDTGSTDSTKEIVSKYTDMVYDFEWIDD----FSAARNFSFSK 72
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLlnqsypKDLI-EIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNpkriQSAGLNIGIRN 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 497584324  73 ASKDYTMWLDADDIILEADREKLLkiKESLDTSIDIV 109
Cdd:cd02525   80 SRGDIIIRVDAHAVYPKDYILELV--EALKRTGADNV 114
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-91 2.70e-11

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 62.32  E-value: 2.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324   1 MITISLCMIVKNEEEVIGRCLECVK---DIVDEIIIVDTGSTDSTKEIVSKYTDMvyDFEWIDD-----FSAARNFSFSK 72
Cdd:COG1216    2 RPKVSVVIPTYNRPELLRRCLESLLaqtYPPFEVIVVDNGSTDGTAELLAALAFP--RVRVIRNpenlgFAAARNLGLRA 79

                         90
                 ....*....|....*....
gi 497584324  73 ASKDYTMWLDaDDIILEAD 91
Cdd:COG1216   80 AGGDYLLFLD-DDTVVEPD 97
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 176-348 7.72e-10

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: 58.97  E-value: 7.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 176 LRIFEKMISegktLEPRHQFYYSR--ELYYNA-RYKEAIEGFTKFLDSSrgwiEDCISACRDLATCYYLINDEKSALYSL 252
Cdd:COG2956   62 IRIHQKLLE----RDPDRAEALLElaQDYLKAgLLDRAEELLEKLLELD----PDDAEALRLLAEIYEQEGDWEKAIEVL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 253 FRSFEFDEPRAEICCDIGKHMFDRQKYKEAIFWYKVALTRDKNDTNggfksndcygyiPSIQLSVCYDRLGESDKAIYYH 332
Cdd:COG2956  134 ERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCAR------------ALLLLAELYLEQGDYEEAIAAL 201

                        170
                 ....*....|....*.
gi 497584324 333 EKTKEIKPNDSAVLHN 348
Cdd:COG2956  202 ERALEQDPDYLPALPR 217
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
189-348 8.76e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.48  E-value: 8.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 189 LEPRH-QFYYSRELYYNA--RYKEAIEGFTKFLDSSRGWIEdcisACRDLATCYYLINDEKSALYSLFRSFEFDEPRAEI 265
Cdd:COG0457    3 LDPDDaEAYNNLGLAYRRlgRYEEAIEDYEKALELDPDDAE----ALYNLGLAYLRLGRYEEALADYEQALELDPDDAEA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 266 CCDIGKHMFDRQKYKEAIFWYKVALTRDKNDTnggfksnDCYGYipsiqLSVCYDRLGESDKAIYYHEKTKEIKPNDSAV 345
Cdd:COG0457   79 LNNLGLALQALGRYEEALEDYDKALELDPDDA-------EALYN-----LGLALLELGRYDEAIEAYERALELDPDDADA 146


                 ...
gi 497584324 346 LHN 348
Cdd:COG0457  147 LYN 149
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 12-144 9.58e-09

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: 54.50  E-value: 9.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324  12 NEEEVIGRCLE-----CVKDIVDEIIIVDTGSTDSTKEIVSKYTDMVYDFEWIddfSAARNF--------SFSKASKDYT 78
Cdd:cd04179    7 NEEENIPELVErllavLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVI---RLSRNFgkgaavraGFKAARGDIV 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497584324  79 MWLDADdiiLEADREKLLK-IKESLDTSIDIVMAKYnvsFDENGNPTLSYYRE-------RLFKRSSNHKWVDP 144
Cdd:cd04179   84 VTMDAD---LQHPPEDIPKlLEKLLEGGADVVIGSR---FVRGGGAGMPLLRRlgsrlfnFLIRLLLGVRISDT 151
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 11-125 2.81e-08

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: 53.00  E-value: 2.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324  11 KNEEEVIGRCLECVKDI---VDEIIIVDTGSTDSTKEIVSKYTDMVYDFEWIDDF------SAARNFSFSKASKDYTMWL 81
Cdd:cd06423    6 YNEEAVIERTIESLLALdypKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDkenggkAGALNAGLRHAKGDIVVVL 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 497584324  82 DADDiILEADREKLLKIKESLDTSIDIVMAKYNVSfdeNGNPTL 125
Cdd:cd06423   86 DADT-ILEPDALKRLVVPFFADPKVGAVQGRVRVR---NGSENL 125
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 30-121 3.35e-08

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 54.28  E-value: 3.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324  30 EIIIVDTGSTDSTKEIVSKYTDMVYDFEWIDD----FSAARNFSFSKASKDYTMWLDADDIILEADREKLLKIKESLDts 105
Cdd:PRK10073  37 EIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQanagVSVARNTGLAVATGKYVAFPDADDVVYPTMYETLMTMALEDD-- 114

                         90
                 ....*....|....*.
gi 497584324 106 IDIVMAKYNVSFDENG 121
Cdd:PRK10073 115 LDVAQCNADWCFRDTG 130
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 29-131 5.81e-07

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: 49.55  E-value: 5.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324  29 DEIIIVDTGSTDSTKEIVSKYTDmVYDFEWIDDFS-----AARNFS--FSKASKDYTMWLDADDIILEADREKLLKIKES 101
Cdd:cd04196   28 DELIISDDGSTDGTVEIIKEYID-KDPFIIILIRNgknlgVARNFEslLQAADGDYVFFCDQDDIWLPDKLERLLKAFLK 106

                         90       100       110
                 ....*....|....*....|....*....|.
gi 497584324 102 lDTSIDIVMAKYNVsFDENGNPT-LSYYRER 131
Cdd:cd04196  107 -DDKPLLVYSDLEL-VDENGNPIgESFFEYQ 135
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 2-146 6.75e-07

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: 49.47  E-value: 6.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324   2 ITISLcmivkNEEEVIGRCLECV-----KDIvdEIIIVDTGSTDSTKEIVSKYTDmvydfeWIDDF--------SAARNF 68
Cdd:cd06433    3 ITPTY-----NQAETLEETIDSVlsqtyPNI--EYIVIDGGSTDGTVDIIKKYED------KITYWisepdkgiYDAMNK 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497584324  69 SFSKASKDYTMWLDADDIILEADREKLLKIKeSLDTSIDIVMAKYNVsFDENGNptLSYYRERLFKRSSNHKWVDPIH 146
Cdd:cd06433   70 GIALATGDIIGFLNSDDTLLPGALLAVVAAF-AEHPEVDVVYGDVLL-VDENGR--VIGRRRPPPFLDKFLLYGMPIC 143
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 10-113 2.57e-06

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: 47.09  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324  10 VKNEEEVIGRCLECVKDIVD------EIIIVDTGSTDSTKEIVSKYTD-----MVYDFewiddfsaARNF--------SF 70
Cdd:cd04187    5 VYNEEENLPELYERLKAVLEslgydyEIIFVDDGSTDRTLEILRELAArdprvKVIRL--------SRNFgqqaallaGL 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 497584324  71 SKASKDYTMWLDADdiiLEADREKLLKIKESLDTSIDIVMAKY 113
Cdd:cd04187   77 DHARGDAVITMDAD---LQDPPELIPEMLAKWEEGYDVVYGVR 116
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 194-342 7.68e-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: 45.18  E-value: 7.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 194 QFYYSRELYYNARYKEAIEGFTKFLDSSRGWIEdcisACRDLATCYYLINDEKSALYSLFRSFEFDEPRAEICCDIGKHM 273
Cdd:COG4783    7 LYALAQALLLAGDYDEAEALLEKALELDPDNPE----AFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLAL 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497584324 274 FDRQKYKEAIFWYKVALTRDKNDTNGGFksndcygyipsiQLSVCYDRLGESDKAIYYHEKTKEIKPND 342
Cdd:COG4783   83 LKAGDYDEALALLEKALKLDPEHPEAYL------------RLARAYRALGRPDEAIAALEKALELDPDD 139
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
176-344 9.78e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 46.54  E-value: 9.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 176 LRIFEKMISegktLEPRH-QFYYSR-ELYYNA-RYKEAIEGFTKFLDSSRgwieDCISACRDLATCYYLINDEKSALYSL 252
Cdd:COG0457   28 IEDYEKALE----LDPDDaEALYNLgLAYLRLgRYEEALADYEQALELDP----DDAEALNNLGLALQALGRYEEALEDY 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 253 FRSFEFDEPRAEICCDIGKHMFDRQKYKEAIFWYKVALTRDKNDTNGGFKsndcygyipsiqLSVCYDRLGESDKAIYYH 332
Cdd:COG0457  100 DKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYN------------LGIALEKLGRYEEALELL 167

                        170
                 ....*....|..
gi 497584324 333 EKTKEIKPNDSA 344
Cdd:COG0457  168 EKLEAAALAALL 179
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 3-45 2.17e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 45.68  E-value: 2.17e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 497584324   3 TISLCMIVKNEEEVIGRCLECVK-----DIVDEIIIVDTGSTDSTKEI 45
Cdd:PRK13915  32 TVSVVLPALNEEETVGKVVDSIRpllmePLVDELIVIDSGSTDATAER 79
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 12-91 2.93e-05

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: 44.11  E-value: 2.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324  12 NEEEVIGRCLECVK---DIVDEIIIVDTGSTDSTKEIVSKY-TDMVYDFE--WIDD--FSAA--RNFSFSKASKDYTMWL 81
Cdd:cd06420    7 NRPEALELVLKSVLnqsILPFEVIIADDGSTEETKELIEEFkSQFPIPIKhvWQEDegFRKAkiRNKAIAAAKGDYLIFI 86

                         90
                 ....*....|
gi 497584324  82 DAdDIILEAD 91
Cdd:cd06420   87 DG-DCIPHPD 95
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 12-48 3.97e-05

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: 44.10  E-value: 3.97e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 497584324  12 NEEEVIGRCLE---CVKDIVDEIIIVDTGSTDSTKEIVSK 48
Cdd:cd02522    9 NEAENLPRLLAslrRLNPLPLEIIVVDGGSTDGTVAIARS 48
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 8-91 8.26e-05

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: 42.55  E-value: 8.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324   8 MIVKNEEEVIGRCLECVK---DIVDEIIIVDTGSTDSTKEIVSKYTDmvyDFEWIDD-----FSAARNFSFSKASKDYTM 79
Cdd:cd04186    3 IVNYNSLEYLKACLDSLLaqtYPDFEVIVVDNASTDGSVELLRELFP---EVRLIRNgenlgFGAGNNQGIREAKGDYVL 79

                         90
                 ....*....|..
gi 497584324  80 WLDaDDIILEAD 91
Cdd:cd04186   80 LLN-PDTVVEPG 90
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 30-108 1.03e-04

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 43.42  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324   30 EIIIVDTGSTDSTKEIVSKYTDM----VYDFEWIDDFS--AARNFSFSKASKDYTMWLDADDIILEADREKLLKIKESLD 103
Cdd:pfam10111  31 ELIIINDGSTDKTLEEVSSIKDHnlqvYYPNAPDTTYSlaASRNRGTSHAIGEYISFIDGDCLWSPDKFEKQLKIATSLA 110


                  ....*
gi 497584324  104 TSIDI 108
Cdd:pfam10111 111 LQENI 115
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 3-51 2.96e-04

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: 41.80  E-value: 2.96e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 497584324   3 TISLCMIVKNEEEVIGRCLECV------KDIVdEIIIVDTGSTDSTKEIVSKYTD 51
Cdd:cd06439   30 TVTIIIPAYNEEAVIEAKLENLlaldypRDRL-EIIVVSDGSTDGTAEIAREYAD 83
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
257-348 3.27e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 41.92  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 257 EFDEPRAEICCDIGKHMFDRQKYKEAIFWYKVALTRDKNDTNGGFksndcygyipsiQLSVCYDRLGESDKAIYYHEKTK 336
Cdd:COG0457    2 ELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALY------------NLGLAYLRLGRYEEALADYEQAL 69

                         90
                 ....*....|..
gi 497584324 337 EIKPNDSAVLHN 348
Cdd:COG0457   70 ELDPDDAEALNN 81
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 199-348 3.40e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 42.67  E-value: 3.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 199 RELYYNARYKEAIEGFTKFLDSSrgwiEDCISACRDLATCYYLINDEKSALYSLFRSFEFDEPRAEICCDIGKHMFDRQK 278
Cdd:COG3914   86 LLLQALGRYEEALALYRRALALN----PDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGR 161

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 279 YKEAIFWYKVALTRDKNDTNggfksndcygyiPSIQLSVCYDRLGESDKAIYYHEKTKEIKPNDSAVLHN 348
Cdd:COG3914  162 LEEAIAALRRALELDPDNAE------------ALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSN 219
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 274-348 8.36e-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: 39.56  E-value: 8.36e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497584324 274 FDRQKYKEAIFWYKVALTRDKNDTNggfksndcygyiPSIQLSVCYDRLGESDKAIYYHEKTKEIKPNDSAVLHN 348
Cdd:COG5010   65 NKLGDFEESLALLEQALQLDPNNPE------------LYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSN 127
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 12-49 1.36e-03

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: 39.47  E-value: 1.36e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 497584324  12 NEEEVIGRCLEcvkDIVD----------EIIIVDTGSTDSTKEIVSKY 49
Cdd:cd04188    7 NEEKRLPPTLE---EAVEyleerpsfsyEIIVVDDGSKDGTAEVARKL 51
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 12-109 3.13e-03

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: 38.67  E-value: 3.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324  12 NEEEVIGRCLE----CVKDIVDEIIIVDTGSTDSTKEIVSKYTDMVYDFEWIDD-----FSAARNFSFSKASKDYTMWLD 82
Cdd:cd06442    7 NERENIPELIErldaALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRpgkrgLGSAYIEGFKAARGDVIVVMD 86

                         90       100
                 ....*....|....*....|....*...
gi 497584324  83 ADdiiLEADREKLLK-IKESLDTSIDIV 109
Cdd:cd06442   87 AD---LSHPPEYIPElLEAQLEGGADLV 111
Glyco_tranf_2_4 pfam13704
Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative ...
 11-87 3.13e-03

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


Pssm-ID: 433416 [Multi-domain]  Cd Length: 97  Bit Score: 36.45  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324   11 KNEEEVIGRCLECVKDI-VDEIIIVDTGSTDSTKEIVSKYTDM-VY-----DFEWIDDFSAARNFSFSKASKDYTMWLDA 83
Cdd:pfam13704   1 RNEADILPQWLAHHLALgFDHIYVYDNGSDDGTAEILARLPDVsILrsdlsYKDARFQVDWRNALLARYAEADWVLVVDA 80


                  ....
gi 497584324   84 DDII 87
Cdd:pfam13704  81 DEFL 84
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
206-293 3.33e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 36.30  E-value: 3.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 206 RYKEAIEGFTKFLDSSRGWIEdcisACRDLATCYYLINDEKSALySLFRSFEFDEPRAEICCDIGKHMFDRQKYKEAIFW 285
Cdd:COG3063    7 DLEEAEEYYEKALELDPDNAD----ALNNLGLLLLEQGRYDEAI-ALEKALKLDPNNAEALLNLAELLLELGDYDEALAY 81


                 ....*...
gi 497584324 286 YKVALTRD 293
Cdd:COG3063   82 LERALELD 89
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 228-348 3.84e-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: 37.09  E-value: 3.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497584324 228 CISACRDLATCYYLINDEKSALYSLFRSFEFDEPRAEICCDIGKHMFDRQKYKEAIFWYKVALTRDKNDTNggfksndcy 307
Cdd:COG4783    3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPE--------- 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 497584324 308 gyiPSIQLSVCYDRLGESDKAIYYHEKTKEIKPNDSAVLHN 348
Cdd:COG4783   74 ---ARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLR 111
 
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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