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Conserved domains on  [gi|4885391|ref|NP_005319|]
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hyaluronan synthase 2 [Homo sapiens]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10157701)

glycosyltransferase family 2 protein similar to Homo sapiens hyaluronan synthase isoenzymes (HAS1, 2, and 3) which catalyze the addition of N-acetyl-d-glucosamine (GlcNAc) or d-glucuronic acid (GlcUA) monosaccharides to the nascent hyaluronan polymer, the terminal step of hyaluronan synthesis

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
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 ...
84-361 1.91e-96

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: 293.01  E-value: 1.91e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391   84 TVALCIAAYQEDPDYLRKCLQSVKRLTypGIKVVMVIDGNSEDDLYMMdifsevmgrdksatyiwknnfhekgpgetdes 163
Cdd:cd06434   1 DVTVIIPVYDEDPDVFRECLRSILRQK--PLEIIVVTDGDDEPYLSIL-------------------------------- 46
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  164 hkessqhvTQLVLSNKSICIMQKWGGKREVMYTAFRALgrSVDYVQVCDSDTMLDPASSVEMVKVLEeDPMVGGVGGDVQ 243
Cdd:cd06434  47 --------SQTVKYGGIFVITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQR 115
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  244 ILNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFVEDWYNQE--FMGNQCSFGDDRHLTNRV 321
Cdd:cd06434 116 ILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEFTNetFMGRRLNAGDDRFLTRYV 195
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 4885391  322 LSLGYATKYTARSKCLTETPIEYLRWLNQQTRWSKSYFRE 361
Cdd:cd06434 196 LSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSNWRS 235
 
Name Accession Description Interval E-value
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
84-361 1.91e-96

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: 293.01  E-value: 1.91e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391   84 TVALCIAAYQEDPDYLRKCLQSVKRLTypGIKVVMVIDGNSEDDLYMMdifsevmgrdksatyiwknnfhekgpgetdes 163
Cdd:cd06434   1 DVTVIIPVYDEDPDVFRECLRSILRQK--PLEIIVVTDGDDEPYLSIL-------------------------------- 46
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  164 hkessqhvTQLVLSNKSICIMQKWGGKREVMYTAFRALgrSVDYVQVCDSDTMLDPASSVEMVKVLEeDPMVGGVGGDVQ 243
Cdd:cd06434  47 --------SQTVKYGGIFVITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQR 115
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  244 ILNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFVEDWYNQE--FMGNQCSFGDDRHLTNRV 321
Cdd:cd06434 116 ILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEFTNetFMGRRLNAGDDRFLTRYV 195
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 4885391  322 LSLGYATKYTARSKCLTETPIEYLRWLNQQTRWSKSYFRE 361
Cdd:cd06434 196 LSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSNWRS 235
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
48-468 1.78e-19

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: 89.03  E-value: 1.78e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391   48 LYGAFLASHLIIQSLFAFLEHRKMKKSLetpiklnKTVALCIAAYQEdPDYLRKCLQSVKRLTYPGIKV-VMVIDGNSED 126
Cdd:COG1215   1 LLLLLALLALLYLLLLALARRRRAPADL-------PRVSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLeVIVVDDGSTD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  127 DLYmmDIFSEVMGRDKSATYIWKnnfhekgpgetdeshkessqhvtqlvlsnksicimQKWGGKREVMYTAFRAlgRSVD 206
Cdd:COG1215  73 ETA--EIARELAAEYPRVRVIER-----------------------------------PENGGKAAALNAGLKA--ARGD 113
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  207 YVQVCDSDTMLDPASSVEMVKVLEeDPMVGgvggdvqilnkydswisflssvrywmafnieracqsyfgcvqcISGPLGM 286
Cdd:COG1215 114 IVVFLDADTVLDPDWLRRLVAAFA-DPGVG-------------------------------------------ASGANLA 149
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  287 YRNSLLHEfVEDWynqefmgNQCSFGDDRHLTNRVLSLGYATKYTARSKCLTETPIEYLRWLNQQTRWSKSYFREWLYNA 366
Cdd:COG1215 150 FRREALEE-VGGF-------DEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHR 221
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  367 MWFHKHHLWMtyeAIITGFFPFFLIATVIQLFYrgkiwnILLFLLTVQLVGLIKssfasclrgniVMVFMSLYSVLYMSS 446
Cdd:COG1215 222 PLLRPRRLLL---FLLLLLLPLLLLLLLLALLA------LLLLLLPALLLALLL-----------ALRRRRLLLPLLHLL 281
                       410       420
                ....*....|....*....|..
gi 4885391  447 LLPAKMFAIATINKAGWGTSGR 468
Cdd:COG1215 282 YGLLLLLAALRGKKVVWKKTPR 303
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
206-357 5.03e-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: 77.88  E-value: 5.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391    206 DYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGVGGDVQILNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLG 285
Cdd:pfam03142 203 EYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGETKIANKRQSWVTAIQVFEYYISHHLSKAFESVFGGVTCLPGCFS 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391    286 MYR-----------------NSLLHEFVEDWYNQEFMGNQCSFGDDRHLTNRVLSL--GYATKYTARSKCLTETPIEYLR 346
Cdd:pfam03142 283 MYRikapkggdgywvpilasPDIVEHYSENVVDTLHKKNLLLLGEDRYLTTLMLKTfpKRKTVFVPQAVCKTIAPDTFKV 362
                         170
                  ....*....|.
gi 4885391    347 WLNQQTRWSKS 357
Cdd:pfam03142 363 LLSQRRRWINS 373
 
Name Accession Description Interval E-value
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
84-361 1.91e-96

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: 293.01  E-value: 1.91e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391   84 TVALCIAAYQEDPDYLRKCLQSVKRLTypGIKVVMVIDGNSEDDLYMMdifsevmgrdksatyiwknnfhekgpgetdes 163
Cdd:cd06434   1 DVTVIIPVYDEDPDVFRECLRSILRQK--PLEIIVVTDGDDEPYLSIL-------------------------------- 46
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  164 hkessqhvTQLVLSNKSICIMQKWGGKREVMYTAFRALgrSVDYVQVCDSDTMLDPASSVEMVKVLEeDPMVGGVGGDVQ 243
Cdd:cd06434  47 --------SQTVKYGGIFVITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQR 115
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  244 ILNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFVEDWYNQE--FMGNQCSFGDDRHLTNRV 321
Cdd:cd06434 116 ILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEFTNetFMGRRLNAGDDRFLTRYV 195
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 4885391  322 LSLGYATKYTARSKCLTETPIEYLRWLNQQTRWSKSYFRE 361
Cdd:cd06434 196 LSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSNWRS 235
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
89-314 6.83e-26

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: 104.23  E-value: 6.83e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391   89 IAAYQEDPDyLRKCLQSVKRLTYPGIKVVmVIDGNSEDDlymmdiFSEVMgRDKSATYIWKNNFHEKGPGetdeshkess 168
Cdd:cd06423   3 VPAYNEEAV-IERTIESLLALDYPKLEVI-VVDDGSTDD------TLEIL-EELAALYIRRVLVVRDKEN---------- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  169 qhvtqlvlsnksicimqkwGGKREVMYTAFRALgrSVDYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGVGGDVQILNKY 248
Cdd:cd06423  64 -------------------GGKAGALNAGLRHA--KGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGS 122
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4885391  249 DSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEfVEDWynqefmgNQCSFGDD 314
Cdd:cd06423 123 ENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAFGAFRREALRE-VGGW-------DEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
48-468 1.78e-19

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: 89.03  E-value: 1.78e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391   48 LYGAFLASHLIIQSLFAFLEHRKMKKSLetpiklnKTVALCIAAYQEdPDYLRKCLQSVKRLTYPGIKV-VMVIDGNSED 126
Cdd:COG1215   1 LLLLLALLALLYLLLLALARRRRAPADL-------PRVSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLeVIVVDDGSTD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  127 DLYmmDIFSEVMGRDKSATYIWKnnfhekgpgetdeshkessqhvtqlvlsnksicimQKWGGKREVMYTAFRAlgRSVD 206
Cdd:COG1215  73 ETA--EIARELAAEYPRVRVIER-----------------------------------PENGGKAAALNAGLKA--ARGD 113
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  207 YVQVCDSDTMLDPASSVEMVKVLEeDPMVGgvggdvqilnkydswisflssvrywmafnieracqsyfgcvqcISGPLGM 286
Cdd:COG1215 114 IVVFLDADTVLDPDWLRRLVAAFA-DPGVG-------------------------------------------ASGANLA 149
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  287 YRNSLLHEfVEDWynqefmgNQCSFGDDRHLTNRVLSLGYATKYTARSKCLTETPIEYLRWLNQQTRWSKSYFREWLYNA 366
Cdd:COG1215 150 FRREALEE-VGGF-------DEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHR 221
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  367 MWFHKHHLWMtyeAIITGFFPFFLIATVIQLFYrgkiwnILLFLLTVQLVGLIKssfasclrgniVMVFMSLYSVLYMSS 446
Cdd:COG1215 222 PLLRPRRLLL---FLLLLLLPLLLLLLLLALLA------LLLLLLPALLLALLL-----------ALRRRRLLLPLLHLL 281
                       410       420
                ....*....|....*....|..
gi 4885391  447 LLPAKMFAIATINKAGWGTSGR 468
Cdd:COG1215 282 YGLLLLLAALRGKKVVWKKTPR 303
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
177-357 4.57e-17

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: 80.81  E-value: 4.57e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  177 SNKSICI-----MQKWGGKR--EVMYtaFRALGRSV-----DYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGVGGDVQI 244
Cdd:cd04190  36 KKIVVCVifdgaIKKNRGKRdsQLWF--FNYFCRVLfpddpEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHP 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  245 LNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYR-------NSLLHEFVEDWYNQEFMG-----NQCSFG 312
Cdd:cd04190 114 MGKKQGPLVMYQVFEYAISHWLDKAFESVFGFVTCLPGCFSMYRiealkgdNGGKGPLLDYAYLTNTVDslhkkNNLDLG 193
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 4885391  313 DDRHLTNRVLSLGYATKYT--ARSKCLTETPIEYLRWLNQQTRWSKS 357
Cdd:cd04190 194 EDRILCTLLLKAGPKRKYLyvPGAVAETDVPETFVELLSQRRRWINS 240
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
206-357 5.03e-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: 77.88  E-value: 5.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391    206 DYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGVGGDVQILNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLG 285
Cdd:pfam03142 203 EYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGETKIANKRQSWVTAIQVFEYYISHHLSKAFESVFGGVTCLPGCFS 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391    286 MYR-----------------NSLLHEFVEDWYNQEFMGNQCSFGDDRHLTNRVLSL--GYATKYTARSKCLTETPIEYLR 346
Cdd:pfam03142 283 MYRikapkggdgywvpilasPDIVEHYSENVVDTLHKKNLLLLGEDRYLTTLMLKTfpKRKTVFVPQAVCKTIAPDTFKV 362
                         170
                  ....*....|.
gi 4885391    347 WLNQQTRWSKS 357
Cdd:pfam03142 363 LLSQRRRWINS 373
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
84-355 2.97e-10

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: 60.46  E-value: 2.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391     84 TVALCIAAYQEDPDYLRkCLQSVKRLTYPGIKVVMVIDGNSEDDLymmDIFSEVMGR--DKSATYIwkNNFHEKGPGetd 161
Cdd:pfam13641   3 DVSVVVPAFNEDSVLGR-VLEAILAQPYPPVEVVVVVNPSDAETL---DVAEEIAARfpDVRLRVI--RNARLLGPT--- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391    162 eshkessqhvtqlvlsnksicimqkwgGKREVMYTAFRALGRsvDYVQVCDSDTMLDPASSVEMVKVLEeDPMVGGVGGD 241
Cdd:pfam13641  74 ---------------------------GKSRGLNHGFRAVKS--DLVVLHDDDSVLHPGTLKKYVQYFD-SPKVGAVGTP 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391    242 VQILNKyDSWISFLSSVRYWMAFnIERACQSYFGCVQCISGPLGMYRNSLLHEFvEDWynqefmGNQCSFGDDRHLTNRV 321
Cdd:pfam13641 124 VFSLNR-STMLSALGALEFALRH-LRMMSLRLALGVLPLSGAGSAIRREVLKEL-GLF------DPFFLLGDDKSLGRRL 194
                         250       260       270
                  ....*....|....*....|....*....|....
gi 4885391    322 LSLGYATKYTARSKCLTETPIEYLRWLNQQTRWS 355
Cdd:pfam13641 195 RRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWV 228
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
82-299 2.01e-09

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 57.79  E-value: 2.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391   82 NKTVALCIAAYQEdPDYLRKCLQSVKRLTYPGIKVVmVIDGNSEDDlyMMDIFSEVMGRDKSATYIWknnfhekgpgetd 161
Cdd:COG0463   1 MPLVSVVIPTYNE-EEYLEEALESLLAQTYPDFEII-VVDDGSTDG--TAEILRELAAKDPRIRVIR------------- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  162 eshkessqhvtqlvlsnksiciMQKWGGKREVMYTAFR-ALGrsvDYVQVCDSDTMLDPASSVEMVKVLEEDPmVGGVGG 240
Cdd:COG0463  64 ----------------------LERNRGKGAARNAGLAaARG---DYIAFLDADDQLDPEKLEELVAALEEGP-ADLVYG 117
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4885391  241 DVQILNKYDSWISFLSSVRYWMAFnieracqsyFGCVQCISGPLGMYRNSLLHE------FVEDW 299
Cdd:COG0463 118 SRLIREGESDLRRLGSRLFNLVRL---------LTNLPDSTSGFRLFRREVLEElgfdegFLEDT 173
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
84-341 1.45e-07

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: 52.58  E-value: 1.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391   84 TVALCIAAYQEDPDYLRKcLQSVKRLTYPG--IKVVMVIDGnSEDDlymmdifsevmgrdksatyiwknnfhekgpgeTD 161
Cdd:cd06439  30 TVTIIIPAYNEEAVIEAK-LENLLALDYPRdrLEIIVVSDG-STDG--------------------------------TA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  162 EshkessqhVTQLVLSNKSICIMQKW-GGKREVMYTAFRALgrSVDYVQVCDSDTMLDPASSVEMVKVLEeDPMVGGVGG 240
Cdd:cd06439  76 E--------IAREYADKGVKLLRFPErRGKAAALNRALALA--TGEIVVFTDANALLDPDALRLLVRHFA-DPSVGAVSG 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  241 DVQILN------------KYDSWIsflssvrywmafnieRACQSYFGCVQCISGPLGMYRNSLLHEFVEDWYNqefmgnq 308
Cdd:cd06439 145 ELVIVDgggsgsgeglywKYENWL---------------KRAESRLGSTVGANGAIYAIRRELFRPLPADTIN------- 202
                       250       260       270
                ....*....|....*....|....*....|...
gi 4885391  309 csfgDDRHLTNRVLSLGYATKYTARSKCLTETP 341
Cdd:cd06439 203 ----DDFVLPLRIARQGYRVVYEPDAVAYEEVA 231
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
87-294 1.92e-05

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 45.08  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391     87 LCIAAYQEdPDYLRKCLQSVKRLTYPGIKVVmVIDGNSEDDLYmmDIFSEVMGRDKSATYIWKNNfhekgpgetdeshke 166
Cdd:pfam00535   2 VIIPTYNE-EKYLLETLESLLNQTYPNFEII-VVDDGSTDGTV--EIAEEYAKKDPRVRVIRLPE--------------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391    167 ssqhvtqlvlsNKsicimqkwgGKREVMYTAFR-ALGrsvDYVQVCDSDTMLDPASSVEMVKVLEEDPmVGGVGGDVQIL 245
Cdd:pfam00535  63 -----------NR---------GKAGARNAGLRaATG---DYIAFLDADDEVPPDWLEKLVEALEEDG-ADVVVGSRYVI 118
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 4885391    246 NKYDSWISFLSSVRYWMAFNIERACQSYFGcVQCISGPLGMYRNSLLHE 294
Cdd:pfam00535 119 FGETGEYRRASRITLSRLPFFLGLRLLGLN-LPFLIGGFALYRREALEE 166
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
89-240 2.51e-05

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: 44.80  E-value: 2.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391   89 IAAYQEdPDYLRKCLQSVKRLTYPGIKVVmVIDGNSEDDlymmdifsevmgrdksaTYIWKNNFHEKGPgetdeshkess 168
Cdd:cd00761   3 IPAYNE-EPYLERCLESLLAQTYPNFEVI-VVDDGSTDG-----------------TLEILEEYAKKDP----------- 52
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4885391  169 qhvtqlvlsNKSICIMQKWGGKREVMYTAFRALgrSVDYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGVGG 240
Cdd:cd00761  53 ---------RVIRVINEENQGLAAARNAGLKAA--RGEYILFLDADDLLLPDWLERLVAELLADPEADAVGG 113
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
84-360 1.68e-04

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: 43.33  E-value: 1.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391   84 TVALCIAAYQEDPDYLRKCLQSVKRLTYPGIKV-VMVID-GNSEDdlymMDIFSEVMGRDKSATYI-WKNNFHEKGpGEt 160
Cdd:cd06421   2 TVDVFIPTYNEPLEIVRKTLRAALAIDYPHDKLrVYVLDdGRRPE----LRALAAELGVEYGYRYLtRPDNRHAKA-GN- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  161 deshkessqhvtqlvLSNksicimqkwggkrevmytafrALGRS-VDYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGvg 239
Cdd:cd06421  76 ---------------LNN---------------------ALAHTtGDFVAILDADHVPTPDFLRRTLGYFLDDPKVAL-- 117
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4885391  240 gdVQILNKYD-----SWIS-FLSSVRYWMAFNIERAcQSYFGCVQCI-SGPLgmYRNSLLHE---FVEDwynqefmgnqc 309
Cdd:cd06421 118 --VQTPQFFYnpdpfDWLAdGAPNEQELFYGVIQPG-RDRWGAAFCCgSGAV--VRREALDEiggFPTD----------- 181
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 4885391  310 SFGDDRHLTNRVLSLGYATKYTARSKCLTETPIEYLRWLNQQTRWSKSYFR 360
Cdd:cd06421 182 SVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQ 232
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
84-127 1.80e-04

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 42.67  E-value: 1.80e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 4885391   84 TVALCIAAYQeDPDYLRKCLQSVKRLTYPGIKVVmVIDGNSEDD 127
Cdd:COG1216   4 KVSVVIPTYN-RPELLRRCLESLLAQTYPPFEVI-VVDNGSTDG 45
 
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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