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Conserved domains on  [gi|661903019|ref|NP_001284365|]
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hyaluronan synthase 1 isoform 2 [Homo sapiens]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
95-385 1.64e-75

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.


The actual alignment was detected with superfamily member cd06434:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 235  Bit Score: 239.46  E-value: 1.64e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019  95 SVALTISAYQEDPAYLRQCLASARALlyprARLRVLMVVDGNRAEDLYMVdmfrevfadedpatyvwdgnyhqpwepaaa 174
Cdd:cd06434    1 DVTVIIPVYDEDPDVFRECLRSILRQ----KPLEIIVVTDGDDEPYLSIL------------------------------ 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 175 gavgagayreveaedpgrlavEALVRTRRCVCVAQRWGGKREVMYTAFKALgdSVDYVQVCDSDTRLDPMALLELVRVLd 254
Cdd:cd06434   47 ---------------------SQTVKYGGIFVITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPF- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 255 EDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFHCVSCISGPLGLYRNNLLQQFLEAWY--NQKFLGTH 332
Cdd:cd06434  103 EDPKVGGVGTNQRILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEftNETFMGRR 182
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 661903019 333 CTFGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWSKSYFRE 385
Cdd:cd06434  183 LNAGDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSNWRS 235
 
Name Accession Description Interval E-value
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
95-385 1.64e-75

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: 239.46  E-value: 1.64e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019  95 SVALTISAYQEDPAYLRQCLASARALlyprARLRVLMVVDGNRAEDLYMVdmfrevfadedpatyvwdgnyhqpwepaaa 174
Cdd:cd06434    1 DVTVIIPVYDEDPDVFRECLRSILRQ----KPLEIIVVTDGDDEPYLSIL------------------------------ 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 175 gavgagayreveaedpgrlavEALVRTRRCVCVAQRWGGKREVMYTAFKALgdSVDYVQVCDSDTRLDPMALLELVRVLd 254
Cdd:cd06434   47 ---------------------SQTVKYGGIFVITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPF- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 255 EDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFHCVSCISGPLGLYRNNLLQQFLEAWY--NQKFLGTH 332
Cdd:cd06434  103 EDPKVGGVGTNQRILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEftNETFMGRR 182
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 661903019 333 CTFGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWSKSYFRE 385
Cdd:cd06434  183 LNAGDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSNWRS 235
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
61-492 1.73e-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: 83.25  E-value: 1.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019  61 FLSAHLVAQSLFAYLehrrvaAAARGPLDAATARSVALTISAYQEdPAYLRQCLASARALLYPRARLRVLMVVDGNRAEd 140
Cdd:COG1215    2 LLLLALLALLYLLLL------ALARRRRAPADLPRVSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDE- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 141 lyMVDMFREVFADEDPATYVwdgnyhqpwepaaagavgagayreveaedpgrlavealvrtrrcvcVAQRWGGKREVMYT 220
Cdd:COG1215   74 --TAEIARELAAEYPRVRVI----------------------------------------------ERPENGGKAAALNA 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 221 AFKAlgDSVDYVQVCDSDTRLDPMALLELVRVLdEDPRVGAvggdvrilnpldswvsflsslrywvafnveracqsyfhc 300
Cdd:COG1215  106 GLKA--ARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGA--------------------------------------- 143
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 301 vsciSGPLGLYRNNLLQQfLEAWynqkflgTHCTFGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWSK 380
Cdd:COG1215  144 ----SGANLAFRREALEE-VGGF-------DEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWAR 211
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 381 SYFREWLYNALWWHRHHAWmtyeavvsgLFPFFVAATVLRLFYAGRPWALLWVLLCVQGVALAKAAFAAWlrgclrmvll 460
Cdd:COG1215  212 GGLQLLLKHRPLLRPRRLL---------LFLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRR---------- 272
                        410       420       430
                 ....*....|....*....|....*....|..
gi 661903019 461 sLYAPLYMCGLLPAKFLALVTMNQSGWGTSGR 492
Cdd:COG1215  273 -LLLPLLHLLYGLLLLLAALRGKKVVWKKTPR 303
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
227-381 1.83e-14

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: 75.95  E-value: 1.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019  227 DSVDYVQVCDSDTRLDPMALLELVRVLDEDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFHCVSCISG 306
Cdd:pfam03142 200 DFYEYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGETKIANKRQSWVTAIQVFEYYISHHLSKAFESVFGGVTCLPG 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019  307 PLGLYRNNLLQQFLEAW------------YNQKFLGT-H----CTFGDDRHLTNRMLSM--GYATKYTSRSRCYSETPSS 367
Cdd:pfam03142 280 CFSMYRIKAPKGGDGYWvpilaspdivehYSENVVDTlHkknlLLLGEDRYLTTLMLKTfpKRKTVFVPQAVCKTIAPDT 359
                         170
                  ....*....|....
gi 661903019  368 FLRWLSQQTRWSKS 381
Cdd:pfam03142 360 FKVLLSQRRRWINS 373
 
Name Accession Description Interval E-value
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
95-385 1.64e-75

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: 239.46  E-value: 1.64e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019  95 SVALTISAYQEDPAYLRQCLASARALlyprARLRVLMVVDGNRAEDLYMVdmfrevfadedpatyvwdgnyhqpwepaaa 174
Cdd:cd06434    1 DVTVIIPVYDEDPDVFRECLRSILRQ----KPLEIIVVTDGDDEPYLSIL------------------------------ 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 175 gavgagayreveaedpgrlavEALVRTRRCVCVAQRWGGKREVMYTAFKALgdSVDYVQVCDSDTRLDPMALLELVRVLd 254
Cdd:cd06434   47 ---------------------SQTVKYGGIFVITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPF- 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 255 EDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFHCVSCISGPLGLYRNNLLQQFLEAWY--NQKFLGTH 332
Cdd:cd06434  103 EDPKVGGVGTNQRILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEftNETFMGRR 182
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 661903019 333 CTFGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWSKSYFRE 385
Cdd:cd06434  183 LNAGDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSNWRS 235
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
212-318 3.30e-22

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: 93.83  E-value: 3.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 212 GGKREVMYTAFKALgdSVDYVQVCDSDTRLDPMALLELVRVLDEDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVE 291
Cdd:cd06423   64 GGKAGALNAGLRHA--KGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLG 141
                         90       100
                 ....*....|....*....|....*..
gi 661903019 292 RACQSYFHCVSCISGPLGLYRNNLLQQ 318
Cdd:cd06423  142 RRAQSALGGVLVLSGAFGAFRREALRE 168
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
61-492 1.73e-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: 83.25  E-value: 1.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019  61 FLSAHLVAQSLFAYLehrrvaAAARGPLDAATARSVALTISAYQEdPAYLRQCLASARALLYPRARLRVLMVVDGNRAEd 140
Cdd:COG1215    2 LLLLALLALLYLLLL------ALARRRRAPADLPRVSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDE- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 141 lyMVDMFREVFADEDPATYVwdgnyhqpwepaaagavgagayreveaedpgrlavealvrtrrcvcVAQRWGGKREVMYT 220
Cdd:COG1215   74 --TAEIARELAAEYPRVRVI----------------------------------------------ERPENGGKAAALNA 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 221 AFKAlgDSVDYVQVCDSDTRLDPMALLELVRVLdEDPRVGAvggdvrilnpldswvsflsslrywvafnveracqsyfhc 300
Cdd:COG1215  106 GLKA--ARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGA--------------------------------------- 143
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 301 vsciSGPLGLYRNNLLQQfLEAWynqkflgTHCTFGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWSK 380
Cdd:COG1215  144 ----SGANLAFRREALEE-VGGF-------DEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWAR 211
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 381 SYFREWLYNALWWHRHHAWmtyeavvsgLFPFFVAATVLRLFYAGRPWALLWVLLCVQGVALAKAAFAAWlrgclrmvll 460
Cdd:COG1215  212 GGLQLLLKHRPLLRPRRLL---------LFLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRR---------- 272
                        410       420       430
                 ....*....|....*....|....*....|..
gi 661903019 461 sLYAPLYMCGLLPAKFLALVTMNQSGWGTSGR 492
Cdd:COG1215  273 -LLLPLLHLLYGLLLLLAALRGKKVVWKKTPR 303
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
227-381 1.83e-14

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: 75.95  E-value: 1.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019  227 DSVDYVQVCDSDTRLDPMALLELVRVLDEDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFHCVSCISG 306
Cdd:pfam03142 200 DFYEYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGETKIANKRQSWVTAIQVFEYYISHHLSKAFESVFGGVTCLPG 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019  307 PLGLYRNNLLQQFLEAW------------YNQKFLGT-H----CTFGDDRHLTNRMLSM--GYATKYTSRSRCYSETPSS 367
Cdd:pfam03142 280 CFSMYRIKAPKGGDGYWvpilaspdivehYSENVVDTlHkknlLLLGEDRYLTTLMLKTfpKRKTVFVPQAVCKTIAPDT 359
                         170
                  ....*....|....
gi 661903019  368 FLRWLSQQTRWSKS 381
Cdd:pfam03142 360 FKVLLSQRRRWINS 373
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
212-381 4.88e-14

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: 71.96  E-value: 4.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 212 GGKR--EVMYtaFKALGDSV-----DYVQVCDSDTRLDPMALLELVRVLDEDPRVGAVGGDVRILNPLDSWVSFLSSLRY 284
Cdd:cd04190   52 RGKRdsQLWF--FNYFCRVLfpddpEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQGPLVMYQVFEY 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 285 WVAFNVERACQSYFHCVSCISGPLGLYR------NNLLQQFLEAW------------YNQKFLgthctfGDDRHLTNRML 346
Cdd:cd04190  130 AISHWLDKAFESVFGFVTCLPGCFSMYRiealkgDNGGKGPLLDYayltntvdslhkKNNLDL------GEDRILCTLLL 203
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 661903019 347 SMGYATKYT--SRSRCYSETPSSFLRWLSQQTRWSKS 381
Cdd:cd04190  204 KAGPKRKYLyvPGAVAETDVPETFVELLSQRRRWINS 240
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
94-379 1.69e-12

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: 67.01  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019   94 RSVALTISAYQEDpAYLRQCLASARALLYPRARLRVlmVVDGNRAEDLYMVDMFREVFADEDPATYVwdgnyhqpwepaa 173
Cdd:pfam13641   2 PDVSVVVPAFNED-SVLGRVLEAILAQPYPPVEVVV--VVNPSDAETLDVAEEIAARFPDVRLRVIR------------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019  174 agavgagayrevEAEDPGRlavealvrtrrcvcvaqrwGGKREVMYTAFKALGDsvDYVQVCDSDTRLDPMALLELVRVL 253
Cdd:pfam13641  66 ------------NARLLGP-------------------TGKSRGLNHGFRAVKS--DLVVLHDDDSVLHPGTLKKYVQYF 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019  254 DeDPRVGAVGGDVRILNPlDSWVSFLSSLRYWVAFNVERACQSYFHcVSCISGPLGLYRNNLLQQFLeawynqKFLGTHC 333
Cdd:pfam13641 113 D-SPKVGAVGTPVFSLNR-STMLSALGALEFALRHLRMMSLRLALG-VLPLSGAGSAIRREVLKELG------LFDPFFL 183
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 661903019  334 tFGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWS 379
Cdd:pfam13641 184 -LGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWV 228
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
89-377 9.36e-12

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: 65.30  E-value: 9.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019  89 DAATARSVALTISAYQEDpAYLRQCLASARALLYPRARLRVLMVVDGNRaedlymvdmfrevfadedpatyvwDGNYhqp 168
Cdd:cd06439   24 DPAYLPTVTIIIPAYNEE-AVIEAKLENLLALDYPRDRLEIIVVSDGST------------------------DGTA--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 169 wepaaagavgaGAYREVEAEDPGRLAVEAlvrtRRcvcvaqrwgGKREVMYTAFKALgdSVDYVQVCDSDTRLDPMALLE 248
Cdd:cd06439   76 -----------EIAREYADKGVKLLRFPE----RR---------GKAAALNRALALA--TGEIVVFTDANALLDPDALRL 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 249 LVRVLdEDPRVGAVGGDVRILNPLDSwvSFLSSLrYWVAFNVERACQSYFHCVSCISGPLGLYRNNLLQQFLEAwynqkf 328
Cdd:cd06439  130 LVRHF-ADPSVGAVSGELVIVDGGGS--GSGEGL-YWKYENWLKRAESRLGSTVGANGAIYAIRRELFRPLPAD------ 199
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 661903019 329 lgthcTFGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTR 377
Cdd:cd06439  200 -----TINDDFVLPLRIARQGYRVVYEPDAVAYEEVAEDGSEEFRRRVR 243
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
236-435 1.40e-06

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: 48.87  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019  236 DSDTRLDPMALLELVRVLdEDPRVGAVGGDVRILNPlDSWVSFLSSLRYWVAFNVERACQSYFHCVSCISGPLGLYRNNL 315
Cdd:pfam13632   6 DADTVLPPDCLLGIANEM-ASPEVAIIQGPILPMNV-GNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAFLRRSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019  316 LQQfleawyNQKFLGTHctFGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWSksyfreWLYNALWWHR 395
Cdd:pfam13632  84 LQE------VGGWDDGS--VSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWA------YGCLLILLIR 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 661903019  396 HHAWmtYEAVVSGLFPFFVAATVLRLFYAGRPWALLWVLL 435
Cdd:pfam13632 150 LLGY--LGTLLWSGLPLALLLLLLFSISSLALVLLLLALL 187
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
94-384 1.97e-06

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: 49.11  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019  94 RSVALTISAYQEDPAYLRQCLASARALLYPRARLRVLMVVDGNRAEdlyMVDMFREVFADEDPATYVWDGNYHqpwepaa 173
Cdd:cd06421    1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPE---LRALAAELGVEYGYRYLTRPDNRH------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 174 agavgagaYREveaedpGRLAvEALVRTRrcvcvaqrwggkrevmytafkalgdsVDYVQVCDSDTRLDPMALLELVRVL 253
Cdd:cd06421   71 --------AKA------GNLN-NALAHTT--------------------------GDFVAILDADHVPTPDFLRRTLGYF 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 254 DEDPRVGAVGG-----DVRILNPLDSWVSflsslrywvafnverACQSYFHCVscisgplglyrnnlLQQFLEAWYNQKF 328
Cdd:cd06421  110 LDDPKVALVQTpqffyNPDPFDWLADGAP---------------NEQELFYGV--------------IQPGRDRWGAAFC 160
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 661903019 329 LGTHC----------------TFGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWSKSYFR 384
Cdd:cd06421  161 CGSGAvvrrealdeiggfptdSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQ 232
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
230-266 1.75e-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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 42.55  E-value: 1.75e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 661903019 230 DYVQVCDSDTRLDPMALLELVRVLDEDPRVGAVGGDV 266
Cdd:cd04186   76 DYVLLLNPDTVVEPGALLELLDAAEQDPDVGIVGPKV 112
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
230-387 5.85e-04

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: 41.86  E-value: 5.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 230 DYVQVCDSDTRLDPMALLELVRVLD-EDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFHCVScisgPL 308
Cdd:cd06427   86 EYVVIYDAEDAPDPDQLKKAVAAFArLDDKLACVQAPLNYYNARENWLTRMFALEYAAWFDYLLPGLARLGLPI----PL 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 309 GLYRNNLLQQFLE---AW--YNqkflgthctFGDDRHLTNRMLSMGYATKyTSRSRCYSETPSSFLRWLSQQTRWSKSYF 383
Cdd:cd06427  162 GGTSNHFRTDVLRelgGWdpFN---------VTEDADLGLRLARAGYRTG-VLNSTTLEEANNALGNWIRQRSRWIKGYM 231

                 ....
gi 661903019 384 REWL 387
Cdd:cd06427  232 QTWL 235
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
209-371 7.72e-04

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 41.23  E-value: 7.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 209 QRWGGKREVMYTAFKALgdSVDYVQVCDSDTRLDPMALLELVRVLDEDPrVGAVGGDVRILNPLDSWVSFLSSLRYWVAF 288
Cdd:COG0463   65 ERNRGKGAARNAGLAAA--RGDYIAFLDADDQLDPEKLEELVAALEEGP-ADLVYGSRLIREGESDLRRLGSRLFNLVRL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019 289 nveracqsyFHCVSCISGPLGLYRNNLLQQfleawynqkfLGTHCTFGDDRHLTnRMLSMGYatKYTSRSRCYSETPSSF 368
Cdd:COG0463  142 ---------LTNLPDSTSGFRLFRREVLEE----------LGFDEGFLEDTELL-RALRHGF--RIAEVPVRYRAGESKL 199

                 ...
gi 661903019 369 LRW 371
Cdd:COG0463  200 NLR 202
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
232-302 1.03e-03

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: 40.44  E-value: 1.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 661903019 232 VQVCDSDTRLDPMALlELVRVLDEDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFHCVS 302
Cdd:cd06436   93 IAVIDADGRLDPNAL-EAVAPYFSDPRVAGTQSRVRMYNRHKNLLTILQDLEFFIIIAATQSLRALTGTVG 162
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
202-269 4.76e-03

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: 37.87  E-value: 4.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 661903019 202 RRCVCVAQRWGGKREVMYTAFKALgdSVDYVQVCDSDTRLDPMALLELVRVLDEDPRVGAVGGDVRIL 269
Cdd:cd00761   53 RVIRVINEENQGLAAARNAGLKAA--RGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNLL 118
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
223-286 5.47e-03

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: 38.35  E-value: 5.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 661903019 223 KALGDSVDYVQVCDSDTRLDPMALLELVRVLDEDPRVgaVGGDVRILNPLDSWVSFLSSLRYWV 286
Cdd:cd06438   76 LNLADDPDAVVVFDADNLVDPNALEELNARFAAGARV--VQAYYNSKNPDDSWITRLYAFAFLV 137
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
230-380 8.29e-03

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: 37.65  E-value: 8.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 661903019  230 DYVQVCDSDTRLDPMALLELVRVLdEDPRVGAVGGDVRILNPldswVSFLSSLRYWVAFNVERACQSYFHCVSCISGPLG 309
Cdd:pfam13506  32 DLLVISDSDIRVPPDYLRDLLAPL-ADPKVGLVTSPPVGSDP----KGLAAALEAAFFNTLAGVLQAALSGIGFAVGMSM 106
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 661903019  310 LYRNNLLQQF--LEAWynqkflgtHCTFGDDRHLTNRMLSMGYATKYTSRSRCYSETP--SSFLRWLSQQTRWSK 380
Cdd:pfam13506 107 AFRRADLERIggFEAL--------ADYLAEDYALGKLLRAAGLKVVLSPRPILQTSGPrrTSFRAFMARQLRWAR 173
 
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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