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Conserved domains on  [gi|27229288|ref|NP_758822|]
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hyaluronan synthase 3 [Rattus norvegicus]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10157701)

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
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
87-365 3.25e-89

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: 274.52  E-value: 3.25e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288  87 SVALCIAAYQEDPEYLRKCLRSAqrIAFPNLKVVMVVDGNRQEDAYMLdifhevlggteqagffvwrsnfheagegetea 166
Cdd:cd06434   1 DVTVIIPVYDEDPDVFRECLRSI--LRQKPLEIIVVTDGDDEPYLSIL-------------------------------- 46
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 167 SLQEGMERVRavvwastfsCIMQKWGGKREVMYTAFKALgnSVDYIQVCDSDTVLDPACTIEMLRVLEeDPQVGGVGGDV 246
Cdd:cd06434  47 SQTVKYGGIF---------VITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQ 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 247 QILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLEDWYH--QKFLGSKCSFGDDRHLTNR 324
Cdd:cd06434 115 RILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEFtnETFMGRRLNAGDDRFLTRY 194
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 27229288 325 VLSLGYRTKYTARSKCLTETPTKYLRWLNQQTRWSKSYFRE 365
Cdd:cd06434 195 VLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSNWRS 235
 
Name Accession Description Interval E-value
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
87-365 3.25e-89

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: 274.52  E-value: 3.25e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288  87 SVALCIAAYQEDPEYLRKCLRSAqrIAFPNLKVVMVVDGNRQEDAYMLdifhevlggteqagffvwrsnfheagegetea 166
Cdd:cd06434   1 DVTVIIPVYDEDPDVFRECLRSI--LRQKPLEIIVVTDGDDEPYLSIL-------------------------------- 46
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 167 SLQEGMERVRavvwastfsCIMQKWGGKREVMYTAFKALgnSVDYIQVCDSDTVLDPACTIEMLRVLEeDPQVGGVGGDV 246
Cdd:cd06434  47 SQTVKYGGIF---------VITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQ 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 247 QILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLEDWYH--QKFLGSKCSFGDDRHLTNR 324
Cdd:cd06434 115 RILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEFtnETFMGRRLNAGDDRFLTRY 194
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 27229288 325 VLSLGYRTKYTARSKCLTETPTKYLRWLNQQTRWSKSYFRE 365
Cdd:cd06434 195 VLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSNWRS 235
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
51-472 2.10e-17

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


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 82.87  E-value: 2.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288  51 ILGLHLLIQSLFAFLEHRRMRRAGRPLKlhcsqrrrSVALCIAAYQEdPEYLRKCLRSAQRIAFPNLKV-VMVVDGNRQE 129
Cdd:COG1215   2 LLLLALLALLYLLLLALARRRRAPADLP--------RVSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLeVIVVDDGSTD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 130 DAYmldifhEVLggteqagffvwrsnfheagegeteASLQEGMERVRAVVwastfsciMQKWGGKREVMYTAFKALGNsv 209
Cdd:COG1215  73 ETA------EIA------------------------RELAAEYPRVRVIE--------RPENGGKAAALNAGLKAARG-- 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 210 DYIQVCDSDTVLDPACTIEMLRVLEeDPQVGgvggdvqilnkydswisflssvrywmafnveracqsyfgcvqcISGPLG 289
Cdd:COG1215 113 DIVVFLDADTVLDPDWLRRLVAAFA-DPGVG-------------------------------------------ASGANL 148
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 290 MYRNSLLQQ---FLEDwyhqkflgskcSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTKYLRWLNQQTRWSKSYFREW 366
Cdd:COG1215 149 AFRREALEEvggFDED-----------TLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLL 217
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 367 LYNSLWFHKHHLWmtyesvvtgFFPFFLIATVIQLFYRGRIWNILLFLLTVQLVGIIKATyacflrgNAEMIFMSLYSLL 446
Cdd:COG1215 218 LKHRPLLRPRRLL---------LFLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLAL-------RRRRLLLPLLHLL 281
                       410       420
                ....*....|....*....|....*.
gi 27229288 447 YMSSLLPAKIFAiatiNKSGWGTSGR 472
Cdd:COG1215 282 YGLLLLLAALRG----KKVVWKKTPR 303
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
86-359 4.74e-17

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: 80.49  E-value: 4.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288    86 RSVALCIAAYQEDPeYLRKCLRSAQRIAFPNLKVVMVVDGNRQEdaymldifhevlggteqagffvwrsnfheagegeTE 165
Cdd:pfam13641   2 PDVSVVVPAFNEDS-VLGRVLEAILAQPYPPVEVVVVVNPSDAE----------------------------------TL 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288   166 ASLQEGMERV-RAVVWASTFSCIMQKwGGKREVMYTAFKALgnSVDYIQVCDSDTVLDPaCTIEMLRVLEEDPQVGGVGG 244
Cdd:pfam13641  47 DVAEEIAARFpDVRLRVIRNARLLGP-TGKSRGLNHGFRAV--KSDLVVLHDDDSVLHP-GTLKKYVQYFDSPKVGAVGT 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288   245 DVQILNKyDSWISFLSSVRYWMAFNVERACQSYFGcVQCISGPLGMYRNSLLQQFlEDWyHQKFLgskcsFGDDRHLTNR 324
Cdd:pfam13641 123 PVFSLNR-STMLSALGALEFALRHLRMMSLRLALG-VLPLSGAGSAIRREVLKEL-GLF-DPFFL-----LGDDKSLGRR 193
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 27229288   325 VLSLGYRTKYTARSKCLTETPTKYLRWLNQQTRWS 359
Cdd:pfam13641 194 LRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWV 228
 
Name Accession Description Interval E-value
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
87-365 3.25e-89

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: 274.52  E-value: 3.25e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288  87 SVALCIAAYQEDPEYLRKCLRSAqrIAFPNLKVVMVVDGNRQEDAYMLdifhevlggteqagffvwrsnfheagegetea 166
Cdd:cd06434   1 DVTVIIPVYDEDPDVFRECLRSI--LRQKPLEIIVVTDGDDEPYLSIL-------------------------------- 46
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 167 SLQEGMERVRavvwastfsCIMQKWGGKREVMYTAFKALgnSVDYIQVCDSDTVLDPACTIEMLRVLEeDPQVGGVGGDV 246
Cdd:cd06434  47 SQTVKYGGIF---------VITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQ 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 247 QILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLEDWYH--QKFLGSKCSFGDDRHLTNR 324
Cdd:cd06434 115 RILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEFtnETFMGRRLNAGDDRFLTRY 194
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 27229288 325 VLSLGYRTKYTARSKCLTETPTKYLRWLNQQTRWSKSYFRE 365
Cdd:cd06434 195 VLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSNWRS 235
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
92-298 2.00e-21

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: 91.52  E-value: 2.00e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288  92 IAAYQEDPEyLRKCLRSAQRIAFPNLKVVMVVDGnrqedayMLDIFHEVLggteqagffvwrsnfheagegeTEASLQEG 171
Cdd:cd06423   3 VPAYNEEAV-IERTIESLLALDYPKLEVIVVDDG-------STDDTLEIL----------------------EELAALYI 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 172 MERVRAVVWAStfscimqkwGGKREVMYTAFKALgnSVDYIQVCDSDTVLDPACTIEMLRVLEEDPQVGGVGGDVQILNK 251
Cdd:cd06423  53 RRVLVVRDKEN---------GGKAGALNAGLRHA--KGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNG 121
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 27229288 252 YDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQ 298
Cdd:cd06423 122 SENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAFGAFRREALRE 168
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
51-472 2.10e-17

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


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 82.87  E-value: 2.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288  51 ILGLHLLIQSLFAFLEHRRMRRAGRPLKlhcsqrrrSVALCIAAYQEdPEYLRKCLRSAQRIAFPNLKV-VMVVDGNRQE 129
Cdd:COG1215   2 LLLLALLALLYLLLLALARRRRAPADLP--------RVSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLeVIVVDDGSTD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 130 DAYmldifhEVLggteqagffvwrsnfheagegeteASLQEGMERVRAVVwastfsciMQKWGGKREVMYTAFKALGNsv 209
Cdd:COG1215  73 ETA------EIA------------------------RELAAEYPRVRVIE--------RPENGGKAAALNAGLKAARG-- 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 210 DYIQVCDSDTVLDPACTIEMLRVLEeDPQVGgvggdvqilnkydswisflssvrywmafnveracqsyfgcvqcISGPLG 289
Cdd:COG1215 113 DIVVFLDADTVLDPDWLRRLVAAFA-DPGVG-------------------------------------------ASGANL 148
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 290 MYRNSLLQQ---FLEDwyhqkflgskcSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTKYLRWLNQQTRWSKSYFREW 366
Cdd:COG1215 149 AFRREALEEvggFDED-----------TLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLL 217
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 367 LYNSLWFHKHHLWmtyesvvtgFFPFFLIATVIQLFYRGRIWNILLFLLTVQLVGIIKATyacflrgNAEMIFMSLYSLL 446
Cdd:COG1215 218 LKHRPLLRPRRLL---------LFLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLAL-------RRRRLLLPLLHLL 281
                       410       420
                ....*....|....*....|....*.
gi 27229288 447 YMSSLLPAKIFAiatiNKSGWGTSGR 472
Cdd:COG1215 282 YGLLLLLAALRG----KKVVWKKTPR 303
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
86-359 4.74e-17

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: 80.49  E-value: 4.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288    86 RSVALCIAAYQEDPeYLRKCLRSAQRIAFPNLKVVMVVDGNRQEdaymldifhevlggteqagffvwrsnfheagegeTE 165
Cdd:pfam13641   2 PDVSVVVPAFNEDS-VLGRVLEAILAQPYPPVEVVVVVNPSDAE----------------------------------TL 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288   166 ASLQEGMERV-RAVVWASTFSCIMQKwGGKREVMYTAFKALgnSVDYIQVCDSDTVLDPaCTIEMLRVLEEDPQVGGVGG 244
Cdd:pfam13641  47 DVAEEIAARFpDVRLRVIRNARLLGP-TGKSRGLNHGFRAV--KSDLVVLHDDDSVLHP-GTLKKYVQYFDSPKVGAVGT 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288   245 DVQILNKyDSWISFLSSVRYWMAFNVERACQSYFGcVQCISGPLGMYRNSLLQQFlEDWyHQKFLgskcsFGDDRHLTNR 324
Cdd:pfam13641 123 PVFSLNR-STMLSALGALEFALRHLRMMSLRLALG-VLPLSGAGSAIRREVLKEL-GLF-DPFFL-----LGDDKSLGRR 193
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 27229288   325 VLSLGYRTKYTARSKCLTETPTKYLRWLNQQTRWS 359
Cdd:pfam13641 194 LRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWV 228
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
92-361 2.04e-15

Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They catalyze chitin synthesis as follows: UDP-N-acetyl-D-glucosamine + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N) <=> UDP + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N+1).


Pssm-ID: 367353 [Multi-domain]  Cd Length: 527  Bit Score: 79.03  E-value: 2.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288    92 IAAYQEDPEYLRKCLRSAQRIAFPNL-KVVMVV-DG-------NRQEDAYMLDIFHEVLGGTEQ---------------- 146
Cdd:pfam03142  31 VTCYSEGEEGLRTTLDSLATTDYPDShKLLLVIcDGmikgsgnDRSTPDIVLDMMKDAVIPKEDpeplsyvavasgskrh 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288   147 ------AGFFVWRSNFHeagegeTEASLQEGMERVRAVVWASTFSCIMQKWG--GKRE-----------VMYTA------ 201
Cdd:pfam03142 111 nmakvyAGFYEYDGDSH------IPEEKQQRVPMIVVVKCGTPSEASEKKPGnrGKRDsqiilmrflqkVHFDErmtple 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288   202 ---FKAL----GNSVDYIQVC---DSDTVLDPACTIEMLRVLEEDPQVGGVGGDVQILNKYDSWISFLSSVRYWMAFNVE 271
Cdd:pfam03142 185 yelFHQIwnvtGVSPDFYEYVlmvDADTKVFPDSLTRMVACMVDDPEIMGLCGETKIANKRQSWVTAIQVFEYYISHHLS 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288   272 RACQSYFGCVQCISGPLGMYR-----------------NSLLQQFLE---DWYHQKFLgskCSFGDDRHLTNRVLSL--G 329
Cdd:pfam03142 265 KAFESVFGGVTCLPGCFSMYRikapkggdgywvpilasPDIVEHYSEnvvDTLHKKNL---LLLGEDRYLTTLMLKTfpK 341
                         330       340       350
                  ....*....|....*....|....*....|..
gi 27229288   330 YRTKYTARSKCLTETPTKYLRWLNQQTRWSKS 361
Cdd:pfam03142 342 RKTVFVPQAVCKTIAPDTFKVLLSQRRRWINS 373
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
187-361 3.06e-15

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: 75.42  E-value: 3.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 187 IMQKWGGKR--EVMYtaFKALGNSV-----DYIQVCDSDTVLDPACTIEMLRVLEEDPQVGGVGGDVQILNKYDSWISFL 259
Cdd:cd04190  47 AIKKNRGKRdsQLWF--FNYFCRVLfpddpEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQGPLVMY 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 260 SSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLEDWYHQKFLGSKCS------------FGDDRHLTNRVLS 327
Cdd:cd04190 125 QVFEYAISHWLDKAFESVFGFVTCLPGCFSMYRIEALKGDNGGKGPLLDYAYLTNtvdslhkknnldLGEDRILCTLLLK 204
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 27229288 328 LGYRTKYT--ARSKCLTETPTKYLRWLNQQTRWSKS 361
Cdd:cd04190 205 AGPKRKYLyvPGAVAETDVPETFVELLSQRRRWINS 240
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
86-364 1.57e-08

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: 55.27  E-value: 1.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288  86 RSVALCIAAYQEDPEYLRKCLRSAQRIAFPNLKVVMVV--DGNRQEDAYMLDIfhevLGGTEQAGFFVWRSNFH-EAGeg 162
Cdd:cd06421   1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYPHDKLRVYVldDGRRPELRALAAE----LGVEYGYRYLTRPDNRHaKAG-- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 163 eteaSLQEGMERVRAvvwastfscimqkwggkrevmytafkalgnsvDYIQVCDSDTVLDPACTIEMLRVLEEDPQVGGv 242
Cdd:cd06421  75 ----NLNNALAHTTG--------------------------------DFVAILDADHVPTPDFLRRTLGYFLDDPKVAL- 117
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 243 ggdVQILNKYD-----SWIsFLSSVRYW-MAFNVERACQSYFGCVQCI-SGPLgmYRNSLLQQ---FLEDwyhqkflgsk 312
Cdd:cd06421 118 ---VQTPQFFYnpdpfDWL-ADGAPNEQeLFYGVIQPGRDRWGAAFCCgSGAV--VRREALDEiggFPTD---------- 181
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 27229288 313 cSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTKYLRWLNQQTRWSKSYFR 364
Cdd:cd06421 182 -SVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQ 232
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
87-348 7.27e-08

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: 53.74  E-value: 7.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288  87 SVALCIAAYQEDpEYLRKCLRSAQRIAFPN--LKVVMVVDGNRqedaymlDIFHEVLGGTEQAGFFVWRsnfHEAGEGET 164
Cdd:cd06439  30 TVTIIIPAYNEE-AVIEAKLENLLALDYPRdrLEIIVVSDGST-------DGTAEIAREYADKGVKLLR---FPERRGKA 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 165 eASLQEGMERVRAvvwastfscimqkwggkrevmytafkalgnsvDYIQVCDSDTVLDPACTIEMLRVLEeDPQVGGVGG 244
Cdd:cd06439  99 -AALNRALALATG--------------------------------EIVVFTDANALLDPDALRLLVRHFA-DPSVGAVSG 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 245 DVQILN------------KYDSWIsflssvrywmafnveRACQSYFGCVQCISGPLGMYRNSLLQQFLEDwyhqkflgsk 312
Cdd:cd06439 145 ELVIVDgggsgsgeglywKYENWL---------------KRAESRLGSTVGANGAIYAIRRELFRPLPAD---------- 199
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 27229288 313 cSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTKY 348
Cdd:cd06439 200 -TINDDFVLPLRIARQGYRVVYEPDAVAYEEVAEDG 234
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
88-334 4.07e-07

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 50.86  E-value: 4.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288  88 VALCIAAYQEdPEYLRKCLRSAQRIAFPNLKVVMVVDGNRqedaymlDIFHEVLggteqagffvwrsnfheagegeteAS 167
Cdd:COG0463   4 VSVVIPTYNE-EEYLEEALESLLAQTYPDFEIIVVDDGST-------DGTAEIL------------------------RE 51
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 168 LQEGMERVRAVVwastfsciMQKWGGKREVMYTAFKALGNsvDYIQVCDSDTVLDPACTIEMLRVLEEDPqVGGVGGDVQ 247
Cdd:COG0463  52 LAAKDPRIRVIR--------LERNRGKGAARNAGLAAARG--DYIAFLDADDQLDPEKLEELVAALEEGP-ADLVYGSRL 120
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288 248 ILNKYDSWISFLSSVRYWMAFnveracqsyFGCVQCISGPLGMYRNSLLQQfledwyhqkfLGSKCSFGDDRHLTnRVLS 327
Cdd:COG0463 121 IREGESDLRRLGSRLFNLVRL---------LTNLPDSTSGFRLFRREVLEE----------LGFDEGFLEDTELL-RALR 180

                ....*..
gi 27229288 328 LGYRTKY 334
Cdd:COG0463 181 HGFRIAE 187
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
211-420 2.93e-04

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: 41.94  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288   211 YIQVCDSDTVLDPACTIEMLRVLEeDPQVGGVGGDVQILNkYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGM 290
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMA-SPEVAIIQGPILPMN-VGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27229288   291 YRNSLLQQfLEDWyhqkflgSKCSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTKYLRWLNQQTRWSKSYFrewlyNS 370
Cdd:pfam13632  79 LRRSALQE-VGGW-------DDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCL-----LI 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 27229288   371 LWFHKHHLWMTYesvVTGFFPFFLIATVIQLFyRGRIWNILLFLLTVQLV 420
Cdd:pfam13632 146 LLIRLLGYLGTL---LWSGLPLALLLLLLFSI-SSLALVLLLLALLAGLL 191
Glucan_BSP_MdoH cd04191
Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic ...
206-240 4.78e-03

Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic Glucan Biosynthesis protein MdoH is a glucosyltransferase that catalyzes the elongation of beta-1,2 polyglucose chains of glucan, requiring a beta-glucoside as a primer and UDP-glucose as a substrate. Glucans are composed of 5 to 10 units of glucose forming a highly branched structure, where beta-1,2-linked glucose constitutes a linear backbone to which branches are attached by beta-1,6 linkages. In Escherichia coli, glucans are located in the periplasmic space, functioning as regulator of osmolarity. It is synthesized at a maximum when cells are grown in a medium with low osmolarity. It has been shown to span the cytoplasmic membrane.


Pssm-ID: 133034 [Multi-domain]  Cd Length: 254  Bit Score: 38.80  E-value: 4.78e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 27229288 206 GNSVDYIQVCDSDTVLDPACTIEMLRVLEEDPQVG 240
Cdd:cd04191  93 GSRYDYMVVLDADSLMSGDTIVRLVRRMEANPRAG 127
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
324-367 5.35e-03

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: 38.78  E-value: 5.35e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 27229288 324 RVLSLGYRTKyTARSKCLTETPTKYLRWLNQQTRWSKSYFREWL 367
Cdd:cd06427 193 RLARAGYRTG-VLNSTTLEEANNALGNWIRQRSRWIKGYMQTWL 235
 
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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