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Conserved domains on  [gi|1622895329|ref|XP_014980199|]
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hyaluronan synthase 1 [Macaca mulatta]

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 ...
192-481 1.28e-74

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: 239.85  E-value: 1.28e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 192 SVALTISAYQEDPAYLRQCLVSARALlyprARLRILMVVDGNRPEDLYMVdmfrevfadedpatyvwdgnyhqpwepaag 271
Cdd:cd06434     1 DVTVIIPVYDEDPDVFRECLRSILRQ----KPLEIIVVTDGDDEPYLSIL------------------------------ 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 272 avgagayreveaedpgrlavEALVRTRRCVCVAQRWGGKREVMYTAFKALgdSVDYVQVCDSDTRLDPMALLELVQVLdE 351
Cdd:cd06434    47 --------------------SQTVKYGGIFVITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPF-E 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 352 DPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFHCVSCISGPLGLYRNNLLQQFLEAWY--NQKFLGTHC 429
Cdd:cd06434   104 DPKVGGVGTNQRILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEftNETFMGRRL 183
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622895329 430 TFGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWSKSYFRE 481
Cdd:cd06434   184 NAGDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSNWRS 235
 
Name Accession Description Interval E-value
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
192-481 1.28e-74

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: 239.85  E-value: 1.28e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 192 SVALTISAYQEDPAYLRQCLVSARALlyprARLRILMVVDGNRPEDLYMVdmfrevfadedpatyvwdgnyhqpwepaag 271
Cdd:cd06434     1 DVTVIIPVYDEDPDVFRECLRSILRQ----KPLEIIVVTDGDDEPYLSIL------------------------------ 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 272 avgagayreveaedpgrlavEALVRTRRCVCVAQRWGGKREVMYTAFKALgdSVDYVQVCDSDTRLDPMALLELVQVLdE 351
Cdd:cd06434    47 --------------------SQTVKYGGIFVITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPF-E 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 352 DPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFHCVSCISGPLGLYRNNLLQQFLEAWY--NQKFLGTHC 429
Cdd:cd06434   104 DPKVGGVGTNQRILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEftNETFMGRRL 183
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622895329 430 TFGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWSKSYFRE 481
Cdd:cd06434   184 NAGDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSNWRS 235
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
192-588 1.16e-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: 84.02  E-value: 1.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 192 SVALTISAYQEdPAYLRQCLVSARALLYPRARLRILMVVDGNRPEdlyMVDMFREVFADEDPATYVwdgnyhqpwepaag 271
Cdd:COG1215    30 RVSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDE---TAEIARELAAEYPRVRVI-------------- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 272 avgagayreveaedpgrlavealvrtrrcvcVAQRWGGKREVMYTAFKAlgDSVDYVQVCDSDTRLDPMALLELVQVLdE 351
Cdd:COG1215    92 -------------------------------ERPENGGKAAALNAGLKA--ARGDIVVFLDADTVLDPDWLRRLVAAF-A 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 352 DPRVGAvggdvrilnpldswvsflsslrywvafnveracqsyfhcvsciSGPLGLYRNNLLQQfLEAWynqkflgTHCTF 431
Cdd:COG1215   138 DPGVGA-------------------------------------------SGANLAFRREALEE-VGGF-------DEDTL 166
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 432 GDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWSKSYFREWLYNALWWHRHHAWmtyeavvsgLFPFFVA 511
Cdd:COG1215   167 GEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRLL---------LFLLLLL 237
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622895329 512 ATVLRLFYAGRPWALLWVLLCVQGVALAKAAFAAWlrgclrmvllsLYAPLYMCGLLPAKFLALVTMNQSGWGTSGR 588
Cdd:COG1215   238 LPLLLLLLLLALLALLLLLLPALLLALLLALRRRR-----------LLLPLLHLLYGLLLLLAALRGKKVVWKKTPR 303
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
197-477 2.22e-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: 79.42  E-value: 2.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 197 ISAYQEDPAYLRQCLVSARALLYPRARLRILMVVDG-------NRPEDLYMVDMFR-EVFADEDP--------------- 253
Cdd:pfam03142  31 VTCYSEGEEGLRTTLDSLATTDYPDSHKLLLVICDGmikgsgnDRSTPDIVLDMMKdAVIPKEDPeplsyvavasgskrh 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 254 -------ATYVWDGNYHQPWE-----PAAGAVGAGAYREVEAEDPG----RLAVEALVRTRRCVCVAQRWGGKREVMYTA 317
Cdd:pfam03142 111 nmakvyaGFYEYDGDSHIPEEkqqrvPMIVVVKCGTPSEASEKKPGnrgkRDSQIILMRFLQKVHFDERMTPLEYELFHQ 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 318 FKAL-GDSVDYVQVC---DSDTRLDPMALLELVQVLDEDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSY 393
Cdd:pfam03142 191 IWNVtGVSPDFYEYVlmvDADTKVFPDSLTRMVACMVDDPEIMGLCGETKIANKRQSWVTAIQVFEYYISHHLSKAFESV 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 394 FHCVSCISGPLGLYRNNLLQQFLEAW------------YNQKFLGT-H----CTFGDDRHLTNRMLSM--GYATKYTSRS 454
Cdd:pfam03142 271 FGGVTCLPGCFSMYRIKAPKGGDGYWvpilaspdivehYSENVVDTlHkknlLLLGEDRYLTTLMLKTfpKRKTVFVPQA 350
                         330       340
                  ....*....|....*....|...
gi 1622895329 455 RCYSETPSSFLRWLSQQTRWSKS 477
Cdd:pfam03142 351 VCKTIAPDTFKVLLSQRRRWINS 373
 
Name Accession Description Interval E-value
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
192-481 1.28e-74

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: 239.85  E-value: 1.28e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 192 SVALTISAYQEDPAYLRQCLVSARALlyprARLRILMVVDGNRPEDLYMVdmfrevfadedpatyvwdgnyhqpwepaag 271
Cdd:cd06434     1 DVTVIIPVYDEDPDVFRECLRSILRQ----KPLEIIVVTDGDDEPYLSIL------------------------------ 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 272 avgagayreveaedpgrlavEALVRTRRCVCVAQRWGGKREVMYTAFKALgdSVDYVQVCDSDTRLDPMALLELVQVLdE 351
Cdd:cd06434    47 --------------------SQTVKYGGIFVITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPF-E 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 352 DPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFHCVSCISGPLGLYRNNLLQQFLEAWY--NQKFLGTHC 429
Cdd:cd06434   104 DPKVGGVGTNQRILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEftNETFMGRRL 183
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622895329 430 TFGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWSKSYFRE 481
Cdd:cd06434   184 NAGDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSNWRS 235
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
308-414 1.22e-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: 95.37  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 308 GGKREVMYTAFKALgdSVDYVQVCDSDTRLDPMALLELVQVLDEDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVE 387
Cdd:cd06423    64 GGKAGALNAGLRHA--KGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLG 141
                          90       100
                  ....*....|....*....|....*..
gi 1622895329 388 RACQSYFHCVSCISGPLGLYRNNLLQQ 414
Cdd:cd06423   142 RRAQSALGGVLVLSGAFGAFRREALRE 168
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
192-588 1.16e-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: 84.02  E-value: 1.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 192 SVALTISAYQEdPAYLRQCLVSARALLYPRARLRILMVVDGNRPEdlyMVDMFREVFADEDPATYVwdgnyhqpwepaag 271
Cdd:COG1215    30 RVSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDE---TAEIARELAAEYPRVRVI-------------- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 272 avgagayreveaedpgrlavealvrtrrcvcVAQRWGGKREVMYTAFKAlgDSVDYVQVCDSDTRLDPMALLELVQVLdE 351
Cdd:COG1215    92 -------------------------------ERPENGGKAAALNAGLKA--ARGDIVVFLDADTVLDPDWLRRLVAAF-A 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 352 DPRVGAvggdvrilnpldswvsflsslrywvafnveracqsyfhcvsciSGPLGLYRNNLLQQfLEAWynqkflgTHCTF 431
Cdd:COG1215   138 DPGVGA-------------------------------------------SGANLAFRREALEE-VGGF-------DEDTL 166
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 432 GDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWSKSYFREWLYNALWWHRHHAWmtyeavvsgLFPFFVA 511
Cdd:COG1215   167 GEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRLL---------LFLLLLL 237
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622895329 512 ATVLRLFYAGRPWALLWVLLCVQGVALAKAAFAAWlrgclrmvllsLYAPLYMCGLLPAKFLALVTMNQSGWGTSGR 588
Cdd:COG1215   238 LPLLLLLLLLALLALLLLLLPALLLALLLALRRRR-----------LLLPLLHLLYGLLLLLAALRGKKVVWKKTPR 303
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
197-477 2.22e-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: 79.42  E-value: 2.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 197 ISAYQEDPAYLRQCLVSARALLYPRARLRILMVVDG-------NRPEDLYMVDMFR-EVFADEDP--------------- 253
Cdd:pfam03142  31 VTCYSEGEEGLRTTLDSLATTDYPDSHKLLLVICDGmikgsgnDRSTPDIVLDMMKdAVIPKEDPeplsyvavasgskrh 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 254 -------ATYVWDGNYHQPWE-----PAAGAVGAGAYREVEAEDPG----RLAVEALVRTRRCVCVAQRWGGKREVMYTA 317
Cdd:pfam03142 111 nmakvyaGFYEYDGDSHIPEEkqqrvPMIVVVKCGTPSEASEKKPGnrgkRDSQIILMRFLQKVHFDERMTPLEYELFHQ 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 318 FKAL-GDSVDYVQVC---DSDTRLDPMALLELVQVLDEDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSY 393
Cdd:pfam03142 191 IWNVtGVSPDFYEYVlmvDADTKVFPDSLTRMVACMVDDPEIMGLCGETKIANKRQSWVTAIQVFEYYISHHLSKAFESV 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 394 FHCVSCISGPLGLYRNNLLQQFLEAW------------YNQKFLGT-H----CTFGDDRHLTNRMLSM--GYATKYTSRS 454
Cdd:pfam03142 271 FGGVTCLPGCFSMYRIKAPKGGDGYWvpilaspdivehYSENVVDTlHkknlLLLGEDRYLTTLMLKTfpKRKTVFVPQA 350
                         330       340
                  ....*....|....*....|...
gi 1622895329 455 RCYSETPSSFLRWLSQQTRWSKS 477
Cdd:pfam03142 351 VCKTIAPDTFKVLLSQRRRWINS 373
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
308-477 1.41e-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: 73.88  E-value: 1.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 308 GGKR--EVMYtaFKALGDSV-----DYVQVCDSDTRLDPMALLELVQVLDEDPRVGAVGGDVRILNPLDSWVSFLSSLRY 380
Cdd:cd04190    52 RGKRdsQLWF--FNYFCRVLfpddpEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQGPLVMYQVFEY 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 381 WVAFNVERACQSYFHCVSCISGPLGLYR------NNLLQQFLEAW------------YNQKFLgthctfGDDRHLTNRML 442
Cdd:cd04190   130 AISHWLDKAFESVFGFVTCLPGCFSMYRiealkgDNGGKGPLLDYayltntvdslhkKNNLDL------GEDRILCTLLL 203
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622895329 443 SMGYATKYT--SRSRCYSETPSSFLRWLSQQTRWSKS 477
Cdd:cd04190   204 KAGPKRKYLyvPGAVAETDVPETFVELLSQRRRWINS 240
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
191-475 2.50e-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: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 191 RSVALTISAYQEDpAYLRQCLVSARALLYPRarLRILMVVDGNRPEDLYMVDMFREVFADEDPATYVwdgnyhqpwepaa 270
Cdd:pfam13641   2 PDVSVVVPAFNED-SVLGRVLEAILAQPYPP--VEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIR------------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 271 gavgagayrevEAEDPGRlavealvrtrrcvcvaqrwGGKREVMYTAFKALGDsvDYVQVCDSDTRLDPMALLELVQVLD 350
Cdd:pfam13641  66 -----------NARLLGP-------------------TGKSRGLNHGFRAVKS--DLVVLHDDDSVLHPGTLKKYVQYFD 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 351 eDPRVGAVGGDVRILNPlDSWVSFLSSLRYWVAFNVERACQSYFHcVSCISGPLGLYRNNLLQQFLeawynqKFLGTHCt 430
Cdd:pfam13641 114 -SPKVGAVGTPVFSLNR-STMLSALGALEFALRHLRMMSLRLALG-VLPLSGAGSAIRREVLKELG------LFDPFFL- 183
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1622895329 431 FGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWS 475
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 ...
192-473 5.41e-11

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: 63.37  E-value: 5.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 192 SVALTISAYQEDpAYLRQCLVSARALLYPRARLRILMVVDGNRpedlymvdmfrevfadedpatyvwDGNYhqpwepaag 271
Cdd:cd06439    30 TVTIIIPAYNEE-AVIEAKLENLLALDYPRDRLEIIVVSDGST------------------------DGTA--------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 272 avgaGAYREVEAEDPGRLAVEAlvrtRRcvcvaqrwgGKREVMYTAFKALgdSVDYVQVCDSDTRLDPMALLELVQVLdE 351
Cdd:cd06439    76 ----EIAREYADKGVKLLRFPE----RR---------GKAAALNRALALA--TGEIVVFTDANALLDPDALRLLVRHF-A 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 352 DPRVGAVGGDVRILNPldSWVSFLSSLrYWVAFNVERACQSYFHCVSCISGPLGLYRNNLLQQFLEAwynqkflgthcTF 431
Cdd:cd06439   136 DPSVGAVSGELVIVDG--GGSGSGEGL-YWKYENWLKRAESRLGSTVGANGAIYAIRRELFRPLPAD-----------TI 201
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1622895329 432 GDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTR 473
Cdd:cd06439   202 NDDFVLPLRIARQGYRVVYEPDAVAYEEVAEDGSEEFRRRVR 243
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
191-480 1.12e-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: 50.26  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 191 RSVALTISAYQEDPAYLRQCLVSARALLYPRARLRILMVVDGNRPEdlyMVDMFREVFADEDPATYVWDGNYHqpwepaa 270
Cdd:cd06421     1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPE---LRALAAELGVEYGYRYLTRPDNRH------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 271 gavgagaYREveaedpGRLAvEALVRTRrcvcvaqrwggkrevmytafkalgdsVDYVQVCDSDTRLDPMALLELVQVLD 350
Cdd:cd06421    71 -------AKA------GNLN-NALAHTT--------------------------GDFVAILDADHVPTPDFLRRTLGYFL 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 351 EDPRVGAVGG-----DVRILNPLDSWVSflsslrywvafnverACQSYFHCVscisgplglyrnnlLQQFLEAWYNQKFL 425
Cdd:cd06421   111 DDPKVALVQTpqffyNPDPFDWLADGAP---------------NEQELFYGV--------------IQPGRDRWGAAFCC 161
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622895329 426 GTHC----------------TFGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWSKSYFR 480
Cdd:cd06421   162 GSGAvvrrealdeiggfptdSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQ 232
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
332-531 1.44e-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: 49.26  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 332 DSDTRLDPMALLELVQVLdEDPRVGAVGGDVRILNPlDSWVSFLSSLRYWVAFNVERACQSYFHCVSCISGPLGLYRNNL 411
Cdd:pfam13632   6 DADTVLPPDCLLGIANEM-ASPEVAIIQGPILPMNV-GNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAFLRRSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 412 LQQfleawyNQKFLGTHctFGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWSksyfreWLYNALWWHR 491
Cdd:pfam13632  84 LQE------VGGWDDGS--VSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWA------YGCLLILLIR 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622895329 492 HHAWmtYEAVVSGLFPFFVAATVLRLFYAGRPWALLWVLL 531
Cdd:pfam13632 150 LLGY--LGTLLWSGLPLALLLLLLFSISSLALVLLLLALL 187
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
326-362 2.78e-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: 42.16  E-value: 2.78e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622895329 326 DYVQVCDSDTRLDPMALLELVQVLDEDPRVGAVGGDV 362
Cdd:cd04186    76 DYVLLLNPDTVVEPGALLELLDAAEQDPDVGIVGPKV 112
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
326-483 2.95e-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: 43.01  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 326 DYVQVCDSDTRLDPMALLELVQVLD-EDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFHCVScisgPL 404
Cdd:cd06427    86 EYVVIYDAEDAPDPDQLKKAVAAFArLDDKLACVQAPLNYYNARENWLTRMFALEYAAWFDYLLPGLARLGLPI----PL 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 405 GLYRNNLLQQFLE---AW--YNqkflgthctFGDDRHLTNRMLSMGYATKyTSRSRCYSETPSSFLRWLSQQTRWSKSYF 479
Cdd:cd06427   162 GGTSNHFRTDVLRelgGWdpFN---------VTEDADLGLRLARAGYRTG-VLNSTTLEEANNALGNWIRQRSRWIKGYM 231

                  ....
gi 1622895329 480 REWL 483
Cdd:cd06427   232 QTWL 235
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
305-467 3.26e-04

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 42.38  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 305 QRWGGKREVMYTAFK-ALGDsvdYVQVCDSDTRLDPMALLELVQVLDEDPrVGAVGGDVRILNPLDSWVSFLSSLRYWVA 383
Cdd:COG0463    65 ERNRGKGAARNAGLAaARGD---YIAFLDADDQLDPEKLEELVAALEEGP-ADLVYGSRLIREGESDLRRLGSRLFNLVR 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 384 FnveracqsyFHCVSCISGPLGLYRNNLLQQfleawynqkfLGTHCTFGDDRHLTnRMLSMGYatKYTSRSRCYSETPSS 463
Cdd:COG0463   141 L---------LTNLPDSTSGFRLFRREVLEE----------LGFDEGFLEDTELL-RALRHGF--RIAEVPVRYRAGESK 198

                  ....
gi 1622895329 464 FLRW 467
Cdd:COG0463   199 LNLR 202
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
328-398 5.91e-04

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: 41.60  E-value: 5.91e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622895329 328 VQVCDSDTRLDPMALLELVQVLDeDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFHCVS 398
Cdd:cd06436    93 IAVIDADGRLDPNALEAVAPYFS-DPRVAGTQSRVRMYNRHKNLLTILQDLEFFIIIAATQSLRALTGTVG 162
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
319-382 2.74e-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: 39.51  E-value: 2.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622895329 319 KALGDSVDYVQVCDSDTRLDPMALLELVQVLDEDPRVgaVGGDVRILNPLDSWVSFLSSLRYWV 382
Cdd:cd06438    76 LNLADDPDAVVVFDADNLVDPNALEELNARFAAGARV--VQAYYNSKNPDDSWITRLYAFAFLV 137
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
298-365 4.12e-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: 38.26  E-value: 4.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622895329 298 RRCVCVAQRWGGKREVMYTAFKALgdSVDYVQVCDSDTRLDPMALLELVQVLDEDPRVGAVGGDVRIL 365
Cdd:cd00761    53 RVIRVINEENQGLAAARNAGLKAA--RGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNLL 118
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
326-476 7.09e-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: 38.03  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622895329 326 DYVQVCDSDTRLDPMALLELVQVLdEDPRVGAVGGDVRILNPldswVSFLSSLRYWVAFNVERACQSYFHCVSCISGPLG 405
Cdd:pfam13506  32 DLLVISDSDIRVPPDYLRDLLAPL-ADPKVGLVTSPPVGSDP----KGLAAALEAAFFNTLAGVLQAALSGIGFAVGMSM 106
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622895329 406 LYRNNLLQQF--LEAWynqkflgtHCTFGDDRHLTNRMLSMGYATKYTSRSRCYSETP--SSFLRWLSQQTRWSK 476
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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