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Conserved domains on  [gi|489826417|ref|WP_003730188|]
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glycosyltransferase [Listeria monocytogenes]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11440297)

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:0006486|GO:0016757
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
53-238 5.69e-65

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: 205.54  E-value: 5.69e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  53 VMVPAHNEGKVIVKTVESLLAFDYPvdRYEIIVINDNSSDNSAELLAAIQAKNPTRFLKIINTDNitggKGKSNALNIGF 132
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYP--KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKEN----GGKAGALNAGL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 133 AESRGELVAIYDADNTPERQALRILVGEITNDAKLGAVIGKFRTRNRDASWLTRFINIETLSFQWMAQAGRWALFKLCTI 212
Cdd:cd06423   75 RHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVL 154
                        170       180
                 ....*....|....*....|....*.
gi 489826417 213 PGTNFIVRRSLLEEIGGWDVKAVAED 238
Cdd:cd06423  155 SGAFGAFRREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
19-361 4.70e-62

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: 202.66  E-value: 4.70e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  19 LLINIVLIVAGYVYYLKneARKVPEIPAEVPFVSVMVPAHNEGKVIVKTVESLLAFDYPVDRYEIIVINDNSSDNSAELL 98
Cdd:COG1215    1 LLLLLALLALLYLLLLA--LARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  99 AAIQAKNPtrFLKIINTDNitgGKGKSNALNIGFAESRGELVAIYDADNTPERQALRILVGEItNDAKLGAvigkfrtrn 178
Cdd:COG1215   79 RELAAEYP--RVRVIERPE---NGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGA--------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 179 rdaswltrfinietlsfqwmaqagrwalfklctiPGTNFIVRRSLLEEIGGWDVKAVAEDTEISFRIYMMGYRIKFQAKA 258
Cdd:COG1215  144 ----------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDA 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 259 VTWEQEPQTLPVWFKQRSRWAKGNIYVILKNVPLLFKRegrrvRFDILYFLSIYFLLLTSLIVSDVLLVLYALGLVHTTL 338
Cdd:COG1215  190 VVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPR-----RLLLFLLLLLLPLLLLLLLLALLALLLLLLPALLLAL 264
                        330       340
                 ....*....|....*....|...
gi 489826417 339 AGLSGALWLLAILLFIAGTFITL 361
Cdd:COG1215  265 LLALRRRRLLLPLLHLLYGLLLL 287
 
Name Accession Description Interval E-value
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
53-238 5.69e-65

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: 205.54  E-value: 5.69e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  53 VMVPAHNEGKVIVKTVESLLAFDYPvdRYEIIVINDNSSDNSAELLAAIQAKNPTRFLKIINTDNitggKGKSNALNIGF 132
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYP--KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKEN----GGKAGALNAGL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 133 AESRGELVAIYDADNTPERQALRILVGEITNDAKLGAVIGKFRTRNRDASWLTRFINIETLSFQWMAQAGRWALFKLCTI 212
Cdd:cd06423   75 RHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVL 154
                        170       180
                 ....*....|....*....|....*.
gi 489826417 213 PGTNFIVRRSLLEEIGGWDVKAVAED 238
Cdd:cd06423  155 SGAFGAFRREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
19-361 4.70e-62

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: 202.66  E-value: 4.70e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  19 LLINIVLIVAGYVYYLKneARKVPEIPAEVPFVSVMVPAHNEGKVIVKTVESLLAFDYPVDRYEIIVINDNSSDNSAELL 98
Cdd:COG1215    1 LLLLLALLALLYLLLLA--LARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  99 AAIQAKNPtrFLKIINTDNitgGKGKSNALNIGFAESRGELVAIYDADNTPERQALRILVGEItNDAKLGAvigkfrtrn 178
Cdd:COG1215   79 RELAAEYP--RVRVIERPE---NGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGA--------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 179 rdaswltrfinietlsfqwmaqagrwalfklctiPGTNFIVRRSLLEEIGGWDVKAVAEDTEISFRIYMMGYRIKFQAKA 258
Cdd:COG1215  144 ----------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDA 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 259 VTWEQEPQTLPVWFKQRSRWAKGNIYVILKNVPLLFKRegrrvRFDILYFLSIYFLLLTSLIVSDVLLVLYALGLVHTTL 338
Cdd:COG1215  190 VVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPR-----RLLLFLLLLLLPLLLLLLLLALLALLLLLLPALLLAL 264
                        330       340
                 ....*....|....*....|...
gi 489826417 339 AGLSGALWLLAILLFIAGTFITL 361
Cdd:COG1215  265 LLALRRRRLLLPLLHLLYGLLLL 287
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
49-281 4.26e-34

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: 126.72  E-value: 4.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417   49 PFVSVMVPAHNEGKVIVKTVESLLAFDYPvdRYEIIVINDNSSDNSAELLAAIQAKNPTRFLKIINTDNITGGKGKSNAL 128
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYP--PVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTGKSRGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  129 NIGFAESRGELVAIYDADNTPERQALRILVgEITNDAKLGAVIGKFRTRNRDASWLT---RFINIETLSFQWMAQAGRWA 205
Cdd:pfam13641  80 NHGFRAVKSDLVVLHDDDSVLHPGTLKKYV-QYFDSPKVGAVGTPVFSLNRSTMLSAlgaLEFALRHLRMMSLRLALGVL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489826417  206 lfklcTIPGTNFIVRRSLLEEIGGWDVK-AVAEDTEISFRIYMMGYRIKFQAKAVTWEQEPQTLPVWFKQRSRWAKG 281
Cdd:pfam13641 159 -----PLSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
49-254 8.82e-30

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 114.41  E-value: 8.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  49 PFVSVMVPAHNEGKVIVKTVESLLAFDYPvdRYEIIVINDNSSDNSAELLAAIQAKNPtrFLKIINTdniTGGKGKSNAL 128
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYP--DFEIIVVDDGSTDGTAEILRELAAKDP--RIRVIRL---ERNRGKGAAR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 129 NIGFAESRGELVAIYDADNTPERQALRILVGEITNDaKLGAVIGKFRTRNRDASWLTRFINIETLsfqwmaqagRWALFK 208
Cdd:COG0463   75 NAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEG-PADLVYGSRLIREGESDLRRLGSRLFNL---------VRLLTN 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489826417 209 LCTIPGTNFIVRRSLLEEIgGWDvKAVAEDTEIsFRIYMMGYRIKF 254
Cdd:COG0463  145 LPDSTSGFRLFRREVLEEL-GFD-EGFLEDTEL-LRALRHGFRIAE 187
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
5-338 3.60e-18

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 87.00  E-value: 3.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417   5 DYLALFAvvciwGLLLIN------IVLIVaGY---VYYLKNEARKVPEIPAEVPFVSVMVPAHNEGKVIVK-TVESLLAF 74
Cdd:PRK11498 213 DPVSLVC-----GLILLFaetyawIVLVL-GYfqvVWPLNRQPVPLPKDMSLWPTVDIFVPTYNEDLNVVKnTIYASLGI 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  75 DYPVDRYEIIVINDNSSDNSAELLAAIQAKNPTRflkiinTDNitgGKGKSNALNIGFAESRGELVAIYDADNTPERQAL 154
Cdd:PRK11498 287 DWPKDKLNIWILDDGGREEFRQFAQEVGVKYIAR------PTH---EHAKAGNINNALKYAKGEFVAIFDCDHVPTRSFL 357
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 155 RILVGEITNDAKLGAV---------------IGKFRtrnrdaswltRFINIETLsFQWMAQAGR--W-ALFkLCtipGTN 216
Cdd:PRK11498 358 QMTMGWFLKDKKLAMMqtphhffspdpfernLGRFR----------KTPNEGTL-FYGLVQDGNdmWdATF-FC---GSC 422
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 217 FIVRRSLLEEIGGWDVKAVAEDTEISFRIYMMGY-----RIKFQAKAVTweqepQTLPVWFKQRSRWAKGNIYVILKNVP 291
Cdd:PRK11498 423 AVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYtsaymRIPQAAGLAT-----ESLSAHIGQRIRWARGMVQIFRLDNP 497
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489826417 292 LLFK--REGRRVRF--DILYFLS-----IY------FLLLTSLIVSD--VLLVLYAL-GLVHTTL 338
Cdd:PRK11498 498 LTGKglKLAQRLCYanAMLHFLSgiprlIFltaplaFLLLHAYIIYApaLMIALFVLpHMIHASL 562
 
Name Accession Description Interval E-value
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
53-238 5.69e-65

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: 205.54  E-value: 5.69e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  53 VMVPAHNEGKVIVKTVESLLAFDYPvdRYEIIVINDNSSDNSAELLAAIQAKNPTRFLKIINTDNitggKGKSNALNIGF 132
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYP--KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKEN----GGKAGALNAGL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 133 AESRGELVAIYDADNTPERQALRILVGEITNDAKLGAVIGKFRTRNRDASWLTRFINIETLSFQWMAQAGRWALFKLCTI 212
Cdd:cd06423   75 RHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVL 154
                        170       180
                 ....*....|....*....|....*.
gi 489826417 213 PGTNFIVRRSLLEEIGGWDVKAVAED 238
Cdd:cd06423  155 SGAFGAFRREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
19-361 4.70e-62

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: 202.66  E-value: 4.70e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  19 LLINIVLIVAGYVYYLKneARKVPEIPAEVPFVSVMVPAHNEGKVIVKTVESLLAFDYPVDRYEIIVINDNSSDNSAELL 98
Cdd:COG1215    1 LLLLLALLALLYLLLLA--LARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  99 AAIQAKNPtrFLKIINTDNitgGKGKSNALNIGFAESRGELVAIYDADNTPERQALRILVGEItNDAKLGAvigkfrtrn 178
Cdd:COG1215   79 RELAAEYP--RVRVIERPE---NGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGA--------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 179 rdaswltrfinietlsfqwmaqagrwalfklctiPGTNFIVRRSLLEEIGGWDVKAVAEDTEISFRIYMMGYRIKFQAKA 258
Cdd:COG1215  144 ----------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDA 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 259 VTWEQEPQTLPVWFKQRSRWAKGNIYVILKNVPLLFKRegrrvRFDILYFLSIYFLLLTSLIVSDVLLVLYALGLVHTTL 338
Cdd:COG1215  190 VVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPR-----RLLLFLLLLLLPLLLLLLLLALLALLLLLLPALLLAL 264
                        330       340
                 ....*....|....*....|...
gi 489826417 339 AGLSGALWLLAILLFIAGTFITL 361
Cdd:COG1215  265 LLALRRRRLLLPLLHLLYGLLLL 287
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
49-281 3.71e-43

CESA_like_2 is a member of 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: 133049 [Multi-domain]  Cd Length: 241  Bit Score: 151.25  E-value: 3.71e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  49 PFVSVMVPAHNEGKVIVKTVESLLAFDYPVDRYEIIVINDnssDNSAELLAAIQAKNPTRFLKIINTDNiTGGKGKSNAL 128
Cdd:cd06427    1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLLE---EDDEETIAAARALRLPSIFRVVVVPP-SQPRTKPKAC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 129 NIGFAESRGELVAIYDADNTPERQALRILVGEIT-NDAKLGAVIGKFRTRNRDASWLTRFINIE-TLSFQ----WMAQAG 202
Cdd:cd06427   77 NYALAFARGEYVVIYDAEDAPDPDQLKKAVAAFArLDDKLACVQAPLNYYNARENWLTRMFALEyAAWFDyllpGLARLG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 203 rwalfklCTIP--GTNFIVRRSLLEEIGGWDVKAVAEDTEISFRIYMMGYRIKFqAKAVTWEQEPQTLPVWFKQRSRWAK 280
Cdd:cd06427  157 -------LPIPlgGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGV-LNSTTLEEANNALGNWIRQRSRWIK 228

                 .
gi 489826417 281 G 281
Cdd:cd06427  229 G 229
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
49-283 2.71e-41

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 146.18  E-value: 2.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  49 PFVSVMVPAHNEGKVIV-KTVESLLAFDYPVDRYEIIVINDNSSDNSAELLAAIQAKNPTRFLKiinTDNITGGK-Gksn 126
Cdd:cd06421    1 PTVDVFIPTYNEPLEIVrKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEYGYRYLT---RPDNRHAKaG--- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 127 ALNIGFAESRGELVAIYDADNTPERQALRILVGEITNDAKLGAVIG-KFRTRNRDASWLTRFINIETLSF-QWMAQAGRW 204
Cdd:cd06421   75 NLNNALAHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTpQFFYNPDPFDWLADGAPNEQELFyGVIQPGRDR 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489826417 205 ALFKLCTipGTNFIVRRSLLEEIGGWDVKAVAEDTEISFRIYMMGYRIKFQAKAVTWEQEPQTLPVWFKQRSRWAKGNI 283
Cdd:cd06421  155 WGAAFCC--GSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGML 231
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
28-283 1.86e-34

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: 128.47  E-value: 1.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  28 AGYVYYLKNEARKVPEIP-----AEVPFVSVMVPAHNEGKVIVKTVESLLAFDYPVDRYEIIVINDNSSDNSAELLAAIQ 102
Cdd:cd06439    3 FGYPLLLKLLARLRPKPPslpdpAYLPTVTIIIPAYNEEAVIEAKLENLLALDYPRDRLEIIVVSDGSTDGTAEIAREYA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 103 AKNptrFLKIINTDNitggKGKSNALNIGFAESRGELVAIYDADNTPERQALRILVgEITNDAKLGAVIGKFRTRNRDAS 182
Cdd:cd06439   83 DKG---VKLLRFPER----RGKAAALNRALALATGEIVVFTDANALLDPDALRLLV-RHFADPSVGAVSGELVIVDGGGS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 183 -------WltRFinietlsFQWMAQA-GRwalfkLCTIPGTN---FIVRRSLLEeigGWDVKAVAEDTEISFRIYMMGYR 251
Cdd:cd06439  155 gsgeglyW--KY-------ENWLKRAeSR-----LGSTVGANgaiYAIRRELFR---PLPADTINDDFVLPLRIARQGYR 217
                        250       260       270
                 ....*....|....*....|....*....|..
gi 489826417 252 IKFQAKAVTWEQEPQTLPVWFKQRSRWAKGNI 283
Cdd:cd06439  218 VVYEPDAVAYEEVAEDGSEEFRRRVRIAAGNL 249
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
49-281 4.26e-34

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: 126.72  E-value: 4.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417   49 PFVSVMVPAHNEGKVIVKTVESLLAFDYPvdRYEIIVINDNSSDNSAELLAAIQAKNPTRFLKIINTDNITGGKGKSNAL 128
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYP--PVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTGKSRGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  129 NIGFAESRGELVAIYDADNTPERQALRILVgEITNDAKLGAVIGKFRTRNRDASWLT---RFINIETLSFQWMAQAGRWA 205
Cdd:pfam13641  80 NHGFRAVKSDLVVLHDDDSVLHPGTLKKYV-QYFDSPKVGAVGTPVFSLNRSTMLSAlgaLEFALRHLRMMSLRLALGVL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489826417  206 lfklcTIPGTNFIVRRSLLEEIGGWDVK-AVAEDTEISFRIYMMGYRIKFQAKAVTWEQEPQTLPVWFKQRSRWAKG 281
Cdd:pfam13641 159 -----PLSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
49-281 2.21e-31

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 119.72  E-value: 2.21e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  49 PFVSVMVPAHNEGKVIVKTVESLLAFDYPVDRYEIIVInDNSSDNSAELLAAIQAKnptRFLKIINTDNITGG--KG-KS 125
Cdd:cd06437    1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVL-DDSTDETVRLAREIVEE---YAAQGVNIKHVRRAdrTGyKA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 126 NALNIGFAESRGELVAIYDADNTPERQALRILVGEItNDAKLGAVIGKFRTRNRDASWLTRFINIETLSFQWMAQAGRWA 205
Cdd:cd06437   77 GALAEGMKVAKGEYVAIFDADFVPPPDFLQKTPPYF-ADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSS 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489826417 206 LFKLCTIPGTNFIVRRSLLEEIGGWDVKAVAEDTEISFRIYMMGYRIKFQAKAVTWEQEPQTLPVWFKQRSRWAKG 281
Cdd:cd06437  156 TGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKG 231
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
53-240 7.22e-31

EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier.


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 116.55  E-value: 7.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  53 VMVPAHNEGKVIVKTVESLLAFDYPVDRYEIIVINDNSSDNSAELLAAIQAKNPTRFlkiintDNItgGKGKSNALNIGF 132
Cdd:cd06438    1 ILIPAHNEEAVIGNTVRSLKAQDYPRELYRIFVVADNCTDDTAQVARAAGATVLERH------DPE--RRGKGYALDFGF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 133 AESRG-----ELVAIYDADNTPERQALRILVGEITNDAKlgAVIGKFRTRNRDASWLTRFINIETLSFQWMAQAGRWALF 207
Cdd:cd06438   73 RHLLNladdpDAVVVFDADNLVDPNALEELNARFAAGAR--VVQAYYNSKNPDDSWITRLYAFAFLVFNRLRPLGRSNLG 150
                        170       180       190
                 ....*....|....*....|....*....|...
gi 489826417 208 KLCTIPGTNFIVRRSLLEEIgGWDVKAVAEDTE 240
Cdd:cd06438  151 LSCQLGGTGMCFPWAVLRQA-PWAAHSLTEDLE 182
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
53-281 2.57e-30

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: 116.62  E-value: 2.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  53 VMVPAHNEGKVIVKTVESLLAFDYPVDRYEIIVINDNSSDNSAELLAAIQAKnPTRFLKIINTDNITgGKGKSNALNIGF 132
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYPKEKFEVILVDDHSTDGTVQILEFAAAK-PNFQLKILNNSRVS-ISGKKNALTTAI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 133 AESRGELVAIYDAD-NTPERQALRILVGEITNDAKL--GAVIGKfrtrnRDASWLTRFINIETLSFQwMAQAGRWALFKL 209
Cdd:cd04192   79 KAAKGDWIVTTDADcVVPSNWLLTFVAFIQKEQIGLvaGPVIYF-----KGKSLLAKFQRLDWLSLL-GLIAGSFGLGKP 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489826417 210 CTIPGTNFIVRRSLLEEIGGWD--VKAVAEDTEISFRIYMMGY-RIKFQAK--AVTWEQEPQTLPVWFKQRSRWAKG 281
Cdd:cd04192  153 FMCNGANMAYRKEAFFEVGGFEgnDHIASGDDELLLAKVASKYpKVAYLKNpeALVTTQPVTSWKELLNQRKRWASK 229
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
49-254 8.82e-30

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 114.41  E-value: 8.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  49 PFVSVMVPAHNEGKVIVKTVESLLAFDYPvdRYEIIVINDNSSDNSAELLAAIQAKNPtrFLKIINTdniTGGKGKSNAL 128
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYP--DFEIIVVDDGSTDGTAEILRELAAKDP--RIRVIRL---ERNRGKGAAR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 129 NIGFAESRGELVAIYDADNTPERQALRILVGEITNDaKLGAVIGKFRTRNRDASWLTRFINIETLsfqwmaqagRWALFK 208
Cdd:COG0463   75 NAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEG-PADLVYGSRLIREGESDLRRLGSRLFNL---------VRLLTN 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489826417 209 LCTIPGTNFIVRRSLLEEIgGWDvKAVAEDTEIsFRIYMMGYRIKF 254
Cdd:COG0463  145 LPDSTSGFRLFRREVLEEL-GFD-EGFLEDTEL-LRALRHGFRIAE 187
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
52-226 4.80e-29

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: 111.33  E-value: 4.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417   52 SVMVPAHNEGKVIVKTVESLLAFDYPvdRYEIIVINDNSSDNSAELLAAIQAKNPtRFLKIINTDNitggKGKSNALNIG 131
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP--NFEIIVVDDGSTDGTVEIAEEYAKKDP-RVRVIRLPEN----RGKAGARNAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  132 FAESRGELVAIYDADNTPERQALRILVGEITNDAKlGAVIGKFRTRNRDASWLTRFINIeTLSFQWMAQAGRWALFKLCT 211
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGA-DVVVGSRYVIFGETGEYRRASRI-TLSRLPFFLGLRLLGLNLPF 151
                         170
                  ....*....|....*
gi 489826417  212 IPGTNFIVRRSLLEE 226
Cdd:pfam00535 152 LIGGFALYRREALEE 166
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
50-294 8.18e-28

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: 110.40  E-value: 8.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  50 FVSVMVPAHNEGKVIVKTVESLLAFDYPVDRYEIIVINDNSSDNSAELLAAIQAKNPtrFLKIIntDNItgGKGKSNALN 129
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLNQSYPKDLIEIIVVDGGSTDGTREIVQEYAAKDP--RIRLI--DNP--KRIQSAGLN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 130 IGFAESRGELVAIYDADNT-PERQALRILVGEITNDAKlgAVIGKFRTRNRDASWltrfINIEtlsfqwMAQAGRWAL-- 206
Cdd:cd02525   75 IGIRNSRGDIIIRVDAHAVyPKDYILELVEALKRTGAD--NVGGPMETIGESKFQ----KAIA------VAQSSPLGSgg 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 207 -------FKLCTIPGTNFIV-RRSLLEEIGGWDVKAV-AEDTEISFRIYMMGYRIKFQAKAVTWEQEPQTLPVWFKQRSR 277
Cdd:cd02525  143 sayrggaVKIGYVDTVHHGAyRREVFEKVGGFDESLVrNEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFR 222
                        250       260
                 ....*....|....*....|....*.
gi 489826417 278 WAKGNIYVILKN---------VPLLF 294
Cdd:cd02525  223 YGKWRARTLRKHrkslslrhlLPLAF 248
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
52-288 4.59e-27

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 107.87  E-value: 4.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  52 SVMVPAHNEGKVIVK-TVESLLAFDYPvdRYEIIVINDNSSDNSaeLLAAIQA---KNPTRFlKIINTDNITGGKgkSNA 127
Cdd:cd06435    1 SIHVPCYEEPPEMVKeTLDSLAALDYP--NFEVIVIDNNTKDEA--LWKPVEAhcaQLGERF-RFFHVEPLPGAK--AGA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 128 LNIGFAESRG--ELVAIYDADNTPERQALRILVGEITnDAKLGAVIGKFRTRNRDASWLTRFINIEtlsfqwmaqagrWA 205
Cdd:cd06435   74 LNYALERTAPdaEIIAVIDADYQVEPDWLKRLVPIFD-DPRVGFVQAPQDYRDGEESLFKRMCYAE------------YK 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 206 LFKLCTIP-----------GTNFIVRRSLLEEIGGWDVKAVAEDTEISFRIYMMGYRIKFQAKAVTWEQEPQTLPVWFKQ 274
Cdd:cd06435  141 GFFDIGMVsrnernaiiqhGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQ 220
                        250
                 ....*....|....
gi 489826417 275 RSRWAKGNIYVILK 288
Cdd:cd06435  221 RFRWAYGAVQILKK 234
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
53-254 1.42e-24

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: 98.73  E-value: 1.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  53 VMVPAHNEGKVIVKTVESLLAFDYPvdRYEIIVINDNSSDNSAELLAAIQAKNPTRFlKIINTDNitggKGKSNALNIGF 132
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYP--NFEVIVVDDGSTDGTLEILEEYAKKDPRVI-RVINEEN----QGLAAARNAGL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 133 AESRGELVAIYDADNTPERQALRILVGEITNDAKLGAVIGKfrtrnrdaswltrfinietlsfqwmaqagrwalfklcti 212
Cdd:cd00761   74 KAARGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGP--------------------------------------- 114
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489826417 213 pgTNFIVRRSLLEEIGGWDVKA-VAEDTEISFRIYMMGYRIKF 254
Cdd:cd00761  115 --GNLLFRRELLEEIGGFDEALlSGEEDDDFLLRLLRGGKVAF 155
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
53-189 1.08e-21

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: 91.48  E-value: 1.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  53 VMVPAHNEGKVIVKTVESLLAFDYPVDRYEIIVINDNSSDNSAELLAAIQAKNPTRFLkIINTDNitggKGKSNALNIGF 132
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRV-IRLSRN----FGKGAAVRAGF 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489826417 133 AESRGELVAIYDADNT--PErqALRILVGEITNDaklGA--VIG--KFRTRNRDASWLTRFIN 189
Cdd:cd04179   76 KAARGDIVVTMDADLQhpPE--DIPKLLEKLLEG---GAdvVIGsrFVRGGGAGMPLLRRLGS 133
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
49-296 1.86e-21

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 91.59  E-value: 1.86e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  49 PFVSVMVPAHNEGKVIVKTVESLLAFDYPvdRYEIIVINDNSSDNSAELLAAIQAKNptrfLKIINTDnitGGKGKSNAL 128
Cdd:COG1216    3 PKVSVVIPTYNRPELLRRCLESLLAQTYP--PFEVIVVDNGSTDGTAELLAALAFPR----VRVIRNP---ENLGFAAAR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 129 NIGFAESRGELVAIYDADNTPERQALRILVgeitndaklgavigkfrtrnrdaswltrfinietlsfqwmaqagRWAlfk 208
Cdd:COG1216   74 NLGLRAAGGDYLLFLDDDTVVEPDWLERLL--------------------------------------------AAA--- 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 209 lctipgtNFIVRRSLLEEIGGWDVK--AVAEDTEISFRIYMMGYRIKFQAKAVTWEQEPQTLPVWFKQRsRWAKGNIYVI 286
Cdd:COG1216  107 -------CLLIRREVFEEVGGFDERffLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAY-YLGRNRLLFL 178
                        250
                 ....*....|
gi 489826417 287 LKNVPLLFKR 296
Cdd:COG1216  179 RKHGPRPLLR 188
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
139-335 7.67e-19

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 83.92  E-value: 7.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  139 LVAIYDADNTPERQALRILVGEITnDAKLGAVIGKFRTRNRdASWLTRFINIETLSFQWMAQAGRWALFKLCTIPGTNFI 218
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMA-SPEVAIIQGPILPMNV-GNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  219 VRRSLLEEIGGWDVKAVAEDTEISFRIYMMGYRIKFQAKAVTWEQEPQTLPVWFKQRSRWAKGnIYVILKNVPLLFKReg 298
Cdd:pfam13632  79 LRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYG-CLLILLIRLLGYLG-- 155
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 489826417  299 RRVRFDILYFLSIYFLLLTSLIVSDVLLVLYALGLVH 335
Cdd:pfam13632 156 TLLWSGLPLALLLLLLFSISSLALVLLLLALLAGLLL 192
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
5-338 3.60e-18

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 87.00  E-value: 3.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417   5 DYLALFAvvciwGLLLIN------IVLIVaGY---VYYLKNEARKVPEIPAEVPFVSVMVPAHNEGKVIVK-TVESLLAF 74
Cdd:PRK11498 213 DPVSLVC-----GLILLFaetyawIVLVL-GYfqvVWPLNRQPVPLPKDMSLWPTVDIFVPTYNEDLNVVKnTIYASLGI 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  75 DYPVDRYEIIVINDNSSDNSAELLAAIQAKNPTRflkiinTDNitgGKGKSNALNIGFAESRGELVAIYDADNTPERQAL 154
Cdd:PRK11498 287 DWPKDKLNIWILDDGGREEFRQFAQEVGVKYIAR------PTH---EHAKAGNINNALKYAKGEFVAIFDCDHVPTRSFL 357
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 155 RILVGEITNDAKLGAV---------------IGKFRtrnrdaswltRFINIETLsFQWMAQAGR--W-ALFkLCtipGTN 216
Cdd:PRK11498 358 QMTMGWFLKDKKLAMMqtphhffspdpfernLGRFR----------KTPNEGTL-FYGLVQDGNdmWdATF-FC---GSC 422
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 217 FIVRRSLLEEIGGWDVKAVAEDTEISFRIYMMGY-----RIKFQAKAVTweqepQTLPVWFKQRSRWAKGNIYVILKNVP 291
Cdd:PRK11498 423 AVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYtsaymRIPQAAGLAT-----ESLSAHIGQRIRWARGMVQIFRLDNP 497
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489826417 292 LLFK--REGRRVRF--DILYFLS-----IY------FLLLTSLIVSD--VLLVLYAL-GLVHTTL 338
Cdd:PRK11498 498 LTGKglKLAQRLCYanAMLHFLSgiprlIFltaplaFLLLHAYIIYApaLMIALFVLpHMIHASL 562
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
53-172 9.81e-17

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: 78.38  E-value: 9.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  53 VMVPAHNEGKVIVKTVESLLAF--DYPVDRYEIIVINDNSSDNSAELLAAIQAKNPTRFLKIINTDNitggKGKSNALNI 130
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVEYleERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLTLPKN----RGKGGAVRA 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 489826417 131 GFAESRGELVAIYDADNTPERQALRILVGEITNDaKLGAVIG 172
Cdd:cd04188   77 GMLAARGDYILFADADLATPFEELEKLEEALKTS-GYDIAIG 117
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
53-261 1.22e-16

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: 76.83  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  53 VMVPAHNEGKVIVKTVESLLAFDYPvdRYEIIVINDNSSDNSAELLaaiqAKNPTRFLKIINTDNItgGKGKSNalNIGF 132
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYP--DFEVIVVDNASTDGSVELL----RELFPEVRLIRNGENL--GFGAGN--NQGI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 133 AESRGELVAIYDADNTPERQALRILVGEITNDAKLGAVIGKfrtrnrdaswltrfinietlsfqwmaqagrwalfklctI 212
Cdd:cd04186   71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQDPDVGIVGPK--------------------------------------V 112
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489826417 213 PGTNFIVRRSLLEEIGGWD--VKAVAEDTEISFRIYMMGYRIKFQAKAVTW 261
Cdd:cd04186  113 SGAFLLVRREVFEEVGGFDedFFLYYEDVDLCLRARLAGYRVLYVPQAVIY 163
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
53-187 2.21e-15

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: 73.67  E-value: 2.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  53 VMVPAHNEGKVIVKTVESLL-AFDYPVDRYEIIVINDNSSDNSAELLAAIQAKNPtRFLKIINTDNitggKGKSNALNIG 131
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKaVLESLGYDYEIIFVDDGSTDRTLEILRELAARDP-RVKVIRLSRN----FGQQAALLAG 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489826417 132 FAESRGELVAIYDAD--NTPErqALRILVGEITNDAKLgaVIGKFrtRNRDASWLTRF 187
Cdd:cd04187   76 LDHARGDAVITMDADlqDPPE--LIPEMLAKWEEGYDV--VYGVR--KNRKESWLKRL 127
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
51-295 1.85e-14

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: 72.22  E-value: 1.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  51 VSVMVPAHNEGKVIVKTVESLLAFDYPVDryEIIVINDNSSDNSAELLaaiqaknpTRFLKIIntdnITGGKGKSNALNI 130
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPLPL--EIIVVDGGSTDGTVAIA--------RSAGVVV----ISSPKGRARQMNA 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 131 GFAESRGELVAIYDADNTPERQALRILvgeITNDAKLGAVIGKFRTRNRDASWLTRFInietlsfqwmaqAGRWALFklC 210
Cdd:cd02522   67 GAAAARGDWLLFLHADTRLPPDWDAAI---IETLRADGAVAGAFRLRFDDPGPRLRLL------------ELGANLR--S 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 211 TIPGTNF-----IVRRSLLEEIGGWDVKAVAEDTEISFRIYMMGYRIKFQAKAVT----WEQEpqtlpvwfkqrsrwakG 281
Cdd:cd02522  130 RLFGLPYgdqglFIRRELFEELGGFPELPLMEDVELVRRLRRRGRPALLPSPVTTsarrWERN----------------G 193
                        250
                 ....*....|....
gi 489826417 282 NIYVILKNVPLLFK 295
Cdd:cd02522  194 WLRTTLLNWLLLLL 207
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
53-229 4.14e-14

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 70.49  E-value: 4.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  53 VMVPAHNEGKVIVKTVESLLAFDypvDRYEIIVINDNSSDNSAELlAAIQAKNPTRFLKIINTDNITGGKGksNALNIGF 132
Cdd:cd06436    1 VLVPCLNEEAVIQRTLASLLRNK---PNFLVLVIDDASDDDTAGI-VRLAITDSRVHLLRRHLPNARTGKG--DALNAAY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 133 -----------AESRGELVAIYDADNTPERQALRiLVGEITNDAKLGAVIGKFRTRNRDASWLTRFINIETLSFQWMAQA 201
Cdd:cd06436   75 dqirqilieegADPERVIIAVIDADGRLDPNALE-AVAPYFSDPRVAGTQSRVRMYNRHKNLLTILQDLEFFIIIAATQS 153
                        170       180
                 ....*....|....*....|....*...
gi 489826417 202 GRwALFKLCTIPGTNFIVRRSLLEEIGG 229
Cdd:cd06436  154 LR-ALTGTVGLGGNGQFMRLSALDGLIG 180
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
52-254 3.81e-12

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: 64.87  E-value: 3.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  52 SVMVPAHNEGKVIVKTVESLLAFDYPvdRYEIIVINDNSSDNSAELLAaiqaKNPTRFLKII-NTDnitggKGKSNALNI 130
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYP--NIEYIVIDGGSTDGTVDIIK----KYEDKITYWIsEPD-----KGIYDAMNK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 131 GFAESRGELVAIYDADNTPERQALRILVGEITNDAKLGAVIGkfRTRNRDASWLTRFINIETLSFqwmaqagRWALFKLC 210
Cdd:cd06433   70 GIALATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYG--DVLLVDENGRVIGRRRPPPFL-------DKFLLYGM 140
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 489826417 211 TIPGTNFIVRRSLLEEIGGWDVK-AVAEDTEISFRIYMMGYRIKF 254
Cdd:cd06433  141 PICHQATFFRRSLFEKYGGFDESyRIAADYDLLLRLLLAGKIFKY 185
PRK10073 PRK10073
putative glycosyl transferase; Provisional
49-148 4.33e-11

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 63.53  E-value: 4.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  49 PFVSVMVPAHNEGKVIVKTVESLLAfdYPVDRYEIIVINDNSSDNSAELLAAIQAKNPTrfLKIINTDNitggKGKSNAL 128
Cdd:PRK10073   6 PKLSIIIPLYNAGKDFRAFMESLIA--QTWTALEIIIVNDGSTDNSVEIAKHYAENYPH--VRLLHQAN----AGVSVAR 77
                         90       100
                 ....*....|....*....|
gi 489826417 129 NIGFAESRGELVAIYDADNT 148
Cdd:PRK10073  78 NTGLAVATGKYVAFPDADDV 97
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
120-280 5.02e-11

Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80.


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 61.14  E-value: 5.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  120 GGKGKSNALNIGFAESRGELVAIYDADNTPERQALRILVGEITnDAKLGAVIGKFRTRNRDaSWLTRFINIETLSFQWMA 199
Cdd:pfam13506  14 GVNPKVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLA-DPKVGLVTSPPVGSDPK-GLAAALEAAFFNTLAGVL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  200 QAGrWALFKLCTipGTNFIVRRSLLEEIGGWDVKA--VAEDTEISFRIYMMGYRIKF--QAKAVTWEQEPQTLPVWFKQR 275
Cdd:pfam13506  92 QAA-LSGIGFAV--GMSMAFRRADLERIGGFEALAdyLAEDYALGKLLRAAGLKVVLspRPILQTSGPRRTSFRAFMARQ 168

                  ....*
gi 489826417  276 SRWAK 280
Cdd:pfam13506 169 LRWAR 173
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
50-284 1.69e-10

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 60.73  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  50 FVSVMVPAHNE-GKVIVKTVESLLAfdypVDRYEIIVINDNSSDNSAELLAAiQAKNPTRFlkIINTDNitggKGKSNAL 128
Cdd:cd06434    1 DVTVIIPVYDEdPDVFRECLRSILR----QKPLEIIVVTDGDDEPYLSILSQ-TVKYGGIF--VITVPH----PGKRRAL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 129 NIGFAESRGELVAIYDADNT-PERQALRILVGeiTNDAKLGAVIGKFRTRNRDASWLTRFINIetlsFQWMAqagRWALF 207
Cdd:cd06434   70 AEGIRHVTTDIVVLLDSDTVwPPNALPEMLKP--FEDPKVGGVGTNQRILRPRDSKWSFLAAE----YLERR---NEEIR 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 208 KLCTIPGTNFIV-------RRSLL-----------EEIGGWDVKAvAEDTEISFRIYMMGYRIKFQAKAVTWEQEPQTLP 269
Cdd:cd06434  141 AAMSYDGGVPCLsgrtaayRTEILkdflfleeftnETFMGRRLNA-GDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYK 219
                        250
                 ....*....|....*
gi 489826417 270 VWFKQRSRWAKGNIY 284
Cdd:cd06434  220 KFLKQQLRWSRSNWR 234
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
49-280 5.14e-09

Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 55.68  E-value: 5.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  49 PFVSVMVPAHNEGKVIVKTVESLLAFDYPvdRYEIIVINDNSSDNSAELLAAIQAKNPTRFLKIINTDNITGGKGKSNAL 128
Cdd:cd02520    1 PGVSILKPLCGVDPNLYENLESFFQQDYP--KYEILFCVQDEDDPAIPVVRKLIAKYPNVDARLLIGGEKVGINPKVNNL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 129 NIGFAESRGELVAIYDADNTPERQALRILVgEITNDAKLGAVIGkfrtrnrdaswltrfinietlsfqwmaqagrwalfk 208
Cdd:cd02520   79 IKGYEEARYDILVISDSDISVPPDYLRRMV-APLMDPGVGLVTC------------------------------------ 121
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489826417 209 LCTIPGTNFIvRRSLLEEIGGWDVKA--VAEDTEISFRIYMMGYRIKFQAKAVTWEQEPQTLPVWFKQRSRWAK 280
Cdd:cd02520  122 LCAFGKSMAL-RREVLDAIGGFEAFAdyLAEDYFLGKLIWRLGYRVVLSPYVVMQPLGSTSLASFWRRQLRWSR 194
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
53-146 2.82e-08

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: 54.08  E-value: 2.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  53 VMVPAHNEGKVIVKTVESLLAFDYPVDrYEIIVINDNSSDNSAELLAAIQAKNPTRFLKIintdnITGGKGKSNALNIGF 132
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKGID-YEIIVVDDNSPDGTAEIVRELAKEYPRVRLIV-----RPGKRGLGSAYIEGF 74
                         90
                 ....*....|....
gi 489826417 133 AESRGELVAIYDAD 146
Cdd:cd06442   75 KAARGDVIVVMDAD 88
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
49-232 2.83e-08

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: 53.75  E-value: 2.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  49 PFVSVMVPAHN-EGKVIVKTVESLLAFDYPvdRYEIIVINDNSSDNS-AELLAAIQAKNPtRFLKIINTDNitggKGKSN 126
Cdd:cd04184    1 PLISIVMPVYNtPEKYLREAIESVRAQTYP--NWELCIADDASTDPEvKRVLKKYAAQDP-RIKVVFREEN----GGISA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 127 ALNIGFAESRGELVAIYDADNTPERQALRILVGEITNDAKLGAV---------IGKFRTRNRDASWltrfiNIETLsfqw 197
Cdd:cd04184   74 ATNSALELATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIysdedkideGGKRSEPFFKPDW-----SPDLL---- 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 489826417 198 MAQagrwalfklctipgtNFI-----VRRSLLEEIGGWDV 232
Cdd:cd04184  145 LSQ---------------NYIghllvYRRSLVRQVGGFRE 169
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
50-147 5.35e-08

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 54.39  E-value: 5.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  50 FVSVMVPAHNEGKVIVKTVESLLAF------DYPVDRYEIIVINDNSSDNSAELLA--AIQAKNPTRFLKIINTDNitgG 121
Cdd:PTZ00260  71 DLSIVIPAYNEEDRLPKMLKETIKYlesrsrKDPKFKYEIIIVNDGSKDKTLKVAKdfWRQNINPNIDIRLLSLLR---N 147
                         90       100
                 ....*....|....*....|....*.
gi 489826417 122 KGKSNALNIGFAESRGELVAIYDADN 147
Cdd:PTZ00260 148 KGKGGAVRIGMLASRGKYILMVDADG 173
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
51-189 6.79e-08

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 53.97  E-value: 6.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  51 VSVMVPAHNEGKVIVKTVESLLAFDYPVDR-YEIIVINDNSSDNSAELLAAIQAKNPTRFLKIINTDNItggkGKSNALN 129
Cdd:PRK10714   8 VSVVIPVYNEQESLPELIRRTTAACESLGKeYEILLIDDGSSDNSAEMLVEAAQAPDSHIVAILLNRNY----GQHSAIM 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489826417 130 IGFAESRGELVAIYDAD--NTPERQALRILVGEITNDaklgaVIGKFRtRNRDASWL----TRFIN 189
Cdd:PRK10714  84 AGFSHVTGDLIITLDADlqNPPEEIPRLVAKADEGYD-----VVGTVR-QNRQDSWFrktaSKMIN 143
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
49-146 2.49e-07

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 51.62  E-value: 2.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  49 PFVSVMVPAHNEGKVIVKTVesLLAFDY--PVDRYEIIVINDNSSDNSAELLAAIQaknptrflKIINTDNIT----GGK 122
Cdd:PLN02726   9 MKYSIIVPTYNERLNIALIV--YLIFKAlqDVKDFEIIVVDDGSPDGTQDVVKQLQ--------KVYGEDRILlrprPGK 78
                         90       100
                 ....*....|....*....|....*
gi 489826417 123 -GKSNALNIGFAESRGELVAIYDAD 146
Cdd:PLN02726  79 lGLGTAYIHGLKHASGDFVVIMDAD 103
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
66-252 5.45e-07

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: 50.36  E-value: 5.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  66 KTVESLLAFDYPVDRyeiIVINDNSSDNSAELLAAIQAKNPTRflkIINTDNItgGKGKsnALNIG--FAESRG-ELVAI 142
Cdd:cd02526   12 KLKELLAALAEQVDK---VVVVDNSSGNDIELRLRLNSEKIEL---IHLGENL--GIAK--ALNIGikAALENGaDYVLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 143 YDADNTPE---RQALRILVGEITNDAKLGAVIGKFRTRNRDASwlTRFINIETLSFQWMAQAGRWALFKLCTI-PGTnfI 218
Cdd:cd02526   82 FDQDSVPPpdmVEKLLAYKILSDKNSNIGAVGPRIIDRRTGEN--SPGVRKSGYKLRIQKEGEEGLKEVDFLItSGS--L 157
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489826417 219 VRRSLLEEIGGWDVK----AVaeDTEISFRIYMMGYRI 252
Cdd:cd02526  158 ISLEALEKVGGFDEDlfidYV--DTEWCLRARSKGYKI 193
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
51-146 5.81e-06

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 47.60  E-value: 5.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  51 VSVMVPAHNE----GKVIVkTVESLLAFDYpVDryEIIVINDNSSDNSAELLAAIQAknptrflKIINTDNITGG----K 122
Cdd:PRK13915  33 VSVVLPALNEeetvGKVVD-SIRPLLMEPL-VD--ELIVIDSGSTDATAERAAAAGA-------RVVSREEILPElpprP 101
                         90       100
                 ....*....|....*....|....
gi 489826417 123 GKSNALNIGFAESRGELVAIYDAD 146
Cdd:PRK13915 102 GKGEALWRSLAATTGDIVVFVDAD 125
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
52-257 1.61e-05

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: 46.12  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417   52 SVMVP--AHNEGKVIVKTVesLLAFDYPVDRYEIIVINDNSSDNSAELLAAIQAKNPTRFLKiiNTDNITGGKGKSNalN 129
Cdd:pfam10111   1 SVVIPvyNGEKTHWIQERI--LNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVYYP--NAPDTTYSLAASR--N 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  130 IGFAESRGELVAIYDADN--TP---ERQALRILVGEITNDAKLGAVI---------GKFRTRNRDASWLTRFINietlsf 195
Cdd:pfam10111  75 RGTSHAIGEYISFIDGDClwSPdkfEKQLKIATSLALQENIQAAVVLpvtdlndesSNFLRRGGDLTASGDVLR------ 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489826417  196 QWMAQAGRWALFKLCTipGTNFIVRRSLLEEIGGWDVKAV---AEDTEISFRIymmGYRIKFQAK 257
Cdd:pfam10111 149 DLLVFYSPLAIFFAPN--SSNALINRQAFIEVGGFDESFRghgAEDFDIFLRL---AARYPFVAV 208
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
66-134 3.65e-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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 44.55  E-value: 3.65e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489826417  66 KTVESLLAFDYPVDRyeIIVINDNSSDNSAELLAAIqaKNPTRFLKIINTDNItGGKGksnalniGFAE 134
Cdd:cd04185   14 ECLDALLAQTRPPDH--IIVIDNASTDGTAEWLTSL--GDLDNIVYLRLPENL-GGAG-------GFYE 70
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
53-283 1.06e-04

C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin; Chitin synthase, also called UDP-N-acetyl-D-glucosamine:chitin 4-beta-N-acetylglucosaminyltransferase, catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of GlcNAc residues formed by covalent beta-1,4 linkages. Chitin is an important component of the cell wall of fungi and bacteria and it is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases. Studies with fungi have revealed that most of them contain more than one chitin synthase gene. At least five subclasses of chitin synthases have been identified.


Pssm-ID: 133033 [Multi-domain]  Cd Length: 244  Bit Score: 43.45  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  53 VMVPAHNEGKV-IVKTVESLLAFDYP------VDRYEIIVIndnssdnsaellaaiqaknptrflkIINTDNITGGKGKS 125
Cdd:cd04190    1 VCVTMYNEDEEeLARTLDSILKNDYPfcarggDSWKKIVVC-------------------------VIFDGAIKKNRGKR 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 126 N-------ALNIGFAESRGELVAIYDADNTPERQALRILVGEITNDAKLGAVIGKFRTRNRDASWLTRFINIETLSFQWM 198
Cdd:cd04190   56 DsqlwffnYFCRVLFPDDPEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQGPLVMYQVFEYAISHWL 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 199 AQA------------GRWALFK---LCTIPGTN-FIVRRSLLEEIGGWDVKAV----AEDTEISFRIYMMGYRIKF---- 254
Cdd:cd04190  136 DKAfesvfgfvtclpGCFSMYRieaLKGDNGGKgPLLDYAYLTNTVDSLHKKNnldlGEDRILCTLLLKAGPKRKYlyvp 215
                        250       260
                 ....*....|....*....|....*....
gi 489826417 255 QAKAVTweQEPQTLPVWFKQRSRWAKGNI 283
Cdd:cd04190  216 GAVAET--DVPETFVELLSQRRRWINSTI 242
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
52-254 3.10e-04

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 42.19  E-value: 3.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  52 SVMVPAHNEGK-VIVKTVESLLAFDyPVDRY-EIIVINDNSSDNSAELLAAIQAKNPTRFLKIINTDNitgGKGKSNALN 129
Cdd:cd02510    1 SVIIIFHNEALsTLLRTVHSVINRT-PPELLkEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKK---REGLIRARI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 130 IGFAESRGELVAIYDADNTPERQALRILVGEITNDAKLGA-----VIGKFRTRNRDASWLTRFINIETLSFQWMAQAGRW 204
Cdd:cd02510   77 AGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVcpiidVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEE 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 205 -------ALFKLCTIPGTNFIVRRSLLEEIGGWDVKAV---AEDTEISFRIYMMGYRIKF 254
Cdd:cd02510  157 rrresptAPIRSPTMAGGLFAIDREWFLELGGYDEGMDiwgGENLELSFKVWQCGGSIEI 216
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
52-118 3.27e-04

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


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 41.85  E-value: 3.27e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489826417  52 SVMVPAHNEGKVIVKTVESLLAFDYPVDryEIIVINDNSSDNSAELLAAIQAKNPTRFLKIINTDNI 118
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYKND--ELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGKNL 65
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
49-151 7.42e-04

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 41.13  E-value: 7.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  49 PFVSVMVPAHNEGKVIVKTVESLLAFDYpvDRYEIIVINDNSSdNSAELLAAIQAKNPTRFLKIINTDNitggKGKSNAL 128
Cdd:PRK10018   5 PLISIYMPTWNRQQLAIRAIKSVLRQDY--SNWEMIIVDDCST-SWEQLQQYVTALNDPRITYIHNDIN----SGACAVR 77
                         90       100
                 ....*....|....*....|....*
gi 489826417 129 NIGFAESRGELVAIYDADN--TPER 151
Cdd:PRK10018  78 NQAIMLAQGEYITGIDDDDewTPNR 102
nfrB PRK11234
phage adsorption protein NrfB;
9-359 2.91e-03

phage adsorption protein NrfB;


Pssm-ID: 236884 [Multi-domain]  Cd Length: 727  Bit Score: 40.11  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417   9 LFAVVCIWGLLLINIVLIVAGYVYYLKNEARKVPEIPaevpfVSVMVPAHNEGKVIVKTVESLLA-FDYPvdRYEIIV-- 85
Cdd:PRK11234  28 LFIDVVYWVRRIKRKLSVYRRYPRMSYRELYKPDEKP-----LAIMVPAWNETGVIGNMAELAATtLDYE--NYHIFVgt 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  86 -INDNSSDNSAEllaAIQAKNPTrFLKIINTDniTGGKGKSNALNigfaesrgelvAIYDADNTPERQALRILVGEITND 164
Cdd:PRK11234 101 yPNDPATQADVD---AVCARFPN-VHKVVCAR--PGPTSKADCLN-----------NVLDAITQFERSANFAFAGFILHD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 165 AKlgAVIGKFRTR-------NRDAswltrfINIETLSFQ--W-----MAQAGRWALFKLCTIP------------GTNF- 217
Cdd:PRK11234 164 AE--DVISPMELRlfnylveRKDL------IQIPVYPFEreWthftsGTYIDEFAELHGKDVPvrealagqvpsaGVGTc 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 218 IVRR---SLLEEIGG--WDVKAVAEDTEISFRIYMMGYRIKFQAKAVTWEQE-----------------------PQTLP 269
Cdd:PRK11234 236 FSRRavtALLEDGDGiaFDVQSLTEDYDIGFRLKEKGMREIFVRFPVVDEAKereqrkflqhartsnmicvreyfPDTFS 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417 270 VWFKQRSRWAKG-------NIYVILKNVPLLFKREGRRVRFDILYFLSIYFLLLTslivsdvLLVLYALGLVHTT----L 338
Cdd:PRK11234 316 AAVRQKSRWIIGivfqgfkTLGWTSSLTLNYFLWRDRKGAITNFVSFLAMLLMLQ-------LLLLLLYESLWPDawhfL 388
                        410       420
                 ....*....|....*....|.
gi 489826417 339 AGLSGALWLLAILLFIAGTFI 359
Cdd:PRK11234 389 SIFSGSAWLMTLLWLNFGLMV 409
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
53-151 3.34e-03

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


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 38.59  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489826417  53 VMVPAHNEGKVIVKTVESLLAFDYpVDRYEIIVINDNSSDNSAELLAAIQAK--NPTRFLKIINTDNITgGKGKSNALNI 130
Cdd:cd06913    1 IILPVHNGEQWLDECLESVLQQDF-EGTLELSVFNDASTDKSAEIIEKWRKKleDSGVIVLVGSHNSPS-PKGVGYAKNQ 78
                         90       100
                 ....*....|....*....|...
gi 489826417 131 GFAESRGELVAIYDADNT--PER 151
Cdd:cd06913   79 AIAQSSGRYLCFLDSDDVmmPQR 101
 
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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