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Conserved domains on  [gi|1061975058|ref|NP_001317977|]
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hyaluronan synthase 3 [Mus musculus]

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 ...
87-365 1.37e-88

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: 272.98  E-value: 1.37e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058  87 SVALCIAAYQEDPEYLRKCLRSAqrIAFPNLKVVMVVDGNRQEDTYMLdifhevlggteqagffvwrsnfheagegetea 166
Cdd:cd06434     1 DVTVIIPVYDEDPDVFRECLRSI--LRQKPLEIIVVTDGDDEPYLSIL-------------------------------- 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 167 SLQEGMERVRavvwastfsCIMQKWGGKREVMYTAFKALgnSVDYIQVCDSDTVLDPACTIEMLRVLEeDPQVGGVGGDV 246
Cdd:cd06434    47 SQTVKYGGIF---------VITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQ 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 247 QILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLEDWYH--QKFLGSKCSFGDDRHLTNR 324
Cdd:cd06434   115 RILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEFtnETFMGRRLNAGDDRFLTRY 194
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1061975058 325 VLSLGYRTKYTARSKCLTETPTRYLRWLNQQTRWSKSYFRE 365
Cdd:cd06434   195 VLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSNWRS 235
 
Name Accession Description Interval E-value
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
87-365 1.37e-88

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: 272.98  E-value: 1.37e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058  87 SVALCIAAYQEDPEYLRKCLRSAqrIAFPNLKVVMVVDGNRQEDTYMLdifhevlggteqagffvwrsnfheagegetea 166
Cdd:cd06434     1 DVTVIIPVYDEDPDVFRECLRSI--LRQKPLEIIVVTDGDDEPYLSIL-------------------------------- 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 167 SLQEGMERVRavvwastfsCIMQKWGGKREVMYTAFKALgnSVDYIQVCDSDTVLDPACTIEMLRVLEeDPQVGGVGGDV 246
Cdd:cd06434    47 SQTVKYGGIF---------VITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQ 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 247 QILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLEDWYH--QKFLGSKCSFGDDRHLTNR 324
Cdd:cd06434   115 RILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEFtnETFMGRRLNAGDDRFLTRY 194
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1061975058 325 VLSLGYRTKYTARSKCLTETPTRYLRWLNQQTRWSKSYFRE 365
Cdd:cd06434   195 VLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSNWRS 235
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
51-472 1.60e-18

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: 86.33  E-value: 1.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058  51 ILGLHLLIQSLFAFLEHRRMRRAGRPLKlhcsqrprSVALCIAAYQEdPEYLRKCLRSAQRIAFPNLKV-VMVVDGNRQE 129
Cdd:COG1215     2 LLLLALLALLYLLLLALARRRRAPADLP--------RVSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLeVIVVDDGSTD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 130 DTYmldifhEVLggteqagffvwrsnfheagegeteASLQEGMERVRAVVwastfsciMQKWGGKREVMYTAFKALGNsv 209
Cdd:COG1215    73 ETA------EIA------------------------RELAAEYPRVRVIE--------RPENGGKAAALNAGLKAARG-- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 210 DYIQVCDSDTVLDPACTIEMLRVLEeDPQVGgvggdvqilnkydswisflssvrywmafnveracqsyfgcvqcISGPLG 289
Cdd:COG1215   113 DIVVFLDADTVLDPDWLRRLVAAFA-DPGVG-------------------------------------------ASGANL 148
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 290 MYRNSLLQQ---FLEDwyhqkflgskcSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTRYLRWLNQQTRWSKSYFREW 366
Cdd:COG1215   149 AFRREALEEvggFDED-----------TLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLL 217
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 367 LYNSLWFHKHHLWmtyesvvtgFFPFFLIATVIQLFYRGRIWNILLFLLTVQLVGIIKATyacflrgNAEMIFMSLYSLL 446
Cdd:COG1215   218 LKHRPLLRPRRLL---------LFLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLAL-------RRRRLLLPLLHLL 281
                         410       420
                  ....*....|....*....|....*.
gi 1061975058 447 YMSSLLPAKIFAiatiNKSGWGTSGR 472
Cdd:COG1215   282 YGLLLLLAALRG----KKVVWKKTPR 303
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
85-359 1.26e-17

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 82.03  E-value: 1.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058  85 PRSVALCIAAYQEDPeYLRKCLRSAQRIAFPNLKVVMVVDGNRQEdtymldifhevlggteqagffvwrsnfheagegeT 164
Cdd:pfam13641   1 PPDVSVVVPAFNEDS-VLGRVLEAILAQPYPPVEVVVVVNPSDAE----------------------------------T 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 165 EASLQEGMERV-RAVVWASTFSCIMQKwGGKREVMYTAFKALgnSVDYIQVCDSDTVLDPaCTIEMLRVLEEDPQVGGVG 243
Cdd:pfam13641  46 LDVAEEIAARFpDVRLRVIRNARLLGP-TGKSRGLNHGFRAV--KSDLVVLHDDDSVLHP-GTLKKYVQYFDSPKVGAVG 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 244 GDVQILNKyDSWISFLSSVRYWMAFNVERACQSYFGcVQCISGPLGMYRNSLLQQFlEDWyHQKFLgskcsFGDDRHLTN 323
Cdd:pfam13641 122 TPVFSLNR-STMLSALGALEFALRHLRMMSLRLALG-VLPLSGAGSAIRREVLKEL-GLF-DPFFL-----LGDDKSLGR 192
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1061975058 324 RVLSLGYRTKYTARSKCLTETPTRYLRWLNQQTRWS 359
Cdd:pfam13641 193 RLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWV 228
 
Name Accession Description Interval E-value
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
87-365 1.37e-88

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: 272.98  E-value: 1.37e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058  87 SVALCIAAYQEDPEYLRKCLRSAqrIAFPNLKVVMVVDGNRQEDTYMLdifhevlggteqagffvwrsnfheagegetea 166
Cdd:cd06434     1 DVTVIIPVYDEDPDVFRECLRSI--LRQKPLEIIVVTDGDDEPYLSIL-------------------------------- 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 167 SLQEGMERVRavvwastfsCIMQKWGGKREVMYTAFKALgnSVDYIQVCDSDTVLDPACTIEMLRVLEeDPQVGGVGGDV 246
Cdd:cd06434    47 SQTVKYGGIF---------VITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQ 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 247 QILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLEDWYH--QKFLGSKCSFGDDRHLTNR 324
Cdd:cd06434   115 RILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEFtnETFMGRRLNAGDDRFLTRY 194
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1061975058 325 VLSLGYRTKYTARSKCLTETPTRYLRWLNQQTRWSKSYFRE 365
Cdd:cd06434   195 VLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSNWRS 235
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
92-298 6.24e-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: 93.06  E-value: 6.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058  92 IAAYQEDPEyLRKCLRSAQRIAFPNLKVVmVVDGNRQEDTYmldifhEVLggteqagffvwrsnfheagegeTEASLQEG 171
Cdd:cd06423     3 VPAYNEEAV-IERTIESLLALDYPKLEVI-VVDDGSTDDTL------EIL----------------------EELAALYI 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 172 MERVRAVVWAStfscimqkwGGKREVMYTAFKALgnSVDYIQVCDSDTVLDPACTIEMLRVLEEDPQVGGVGGDVQILNK 251
Cdd:cd06423    53 RRVLVVRDKEN---------GGKAGALNAGLRHA--KGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNG 121
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1061975058 252 YDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQ 298
Cdd:cd06423   122 SENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAFGAFRREALRE 168
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
51-472 1.60e-18

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: 86.33  E-value: 1.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058  51 ILGLHLLIQSLFAFLEHRRMRRAGRPLKlhcsqrprSVALCIAAYQEdPEYLRKCLRSAQRIAFPNLKV-VMVVDGNRQE 129
Cdd:COG1215     2 LLLLALLALLYLLLLALARRRRAPADLP--------RVSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLeVIVVDDGSTD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 130 DTYmldifhEVLggteqagffvwrsnfheagegeteASLQEGMERVRAVVwastfsciMQKWGGKREVMYTAFKALGNsv 209
Cdd:COG1215    73 ETA------EIA------------------------RELAAEYPRVRVIE--------RPENGGKAAALNAGLKAARG-- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 210 DYIQVCDSDTVLDPACTIEMLRVLEeDPQVGgvggdvqilnkydswisflssvrywmafnveracqsyfgcvqcISGPLG 289
Cdd:COG1215   113 DIVVFLDADTVLDPDWLRRLVAAFA-DPGVG-------------------------------------------ASGANL 148
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 290 MYRNSLLQQ---FLEDwyhqkflgskcSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTRYLRWLNQQTRWSKSYFREW 366
Cdd:COG1215   149 AFRREALEEvggFDED-----------TLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLL 217
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 367 LYNSLWFHKHHLWmtyesvvtgFFPFFLIATVIQLFYRGRIWNILLFLLTVQLVGIIKATyacflrgNAEMIFMSLYSLL 446
Cdd:COG1215   218 LKHRPLLRPRRLL---------LFLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLAL-------RRRRLLLPLLHLL 281
                         410       420
                  ....*....|....*....|....*.
gi 1061975058 447 YMSSLLPAKIFAiatiNKSGWGTSGR 472
Cdd:COG1215   282 YGLLLLLAALRG----KKVVWKKTPR 303
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
85-359 1.26e-17

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 82.03  E-value: 1.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058  85 PRSVALCIAAYQEDPeYLRKCLRSAQRIAFPNLKVVMVVDGNRQEdtymldifhevlggteqagffvwrsnfheagegeT 164
Cdd:pfam13641   1 PPDVSVVVPAFNEDS-VLGRVLEAILAQPYPPVEVVVVVNPSDAE----------------------------------T 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 165 EASLQEGMERV-RAVVWASTFSCIMQKwGGKREVMYTAFKALgnSVDYIQVCDSDTVLDPaCTIEMLRVLEEDPQVGGVG 243
Cdd:pfam13641  46 LDVAEEIAARFpDVRLRVIRNARLLGP-TGKSRGLNHGFRAV--KSDLVVLHDDDSVLHP-GTLKKYVQYFDSPKVGAVG 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 244 GDVQILNKyDSWISFLSSVRYWMAFNVERACQSYFGcVQCISGPLGMYRNSLLQQFlEDWyHQKFLgskcsFGDDRHLTN 323
Cdd:pfam13641 122 TPVFSLNR-STMLSALGALEFALRHLRMMSLRLALG-VLPLSGAGSAIRREVLKEL-GLF-DPFFL-----LGDDKSLGR 192
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1061975058 324 RVLSLGYRTKYTARSKCLTETPTRYLRWLNQQTRWS 359
Cdd:pfam13641 193 RLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWV 228
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
92-361 1.68e-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: 1.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058  92 IAAYQEDPEYLRKCLRSAQRIAFPNL-KVVMVV-DG-------NRQEDTYMLDIFHEVLGGTEQ---------------- 146
Cdd:pfam03142  31 VTCYSEGEEGLRTTLDSLATTDYPDShKLLLVIcDGmikgsgnDRSTPDIVLDMMKDAVIPKEDpeplsyvavasgskrh 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 147 ------AGFFVWRSNFHeagegeTEASLQEGMERVRAVVWASTFSCIMQKWG--GKRE-----------VMYTA------ 201
Cdd:pfam03142 111 nmakvyAGFYEYDGDSH------IPEEKQQRVPMIVVVKCGTPSEASEKKPGnrGKRDsqiilmrflqkVHFDErmtple 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 202 ---FKAL----GNSVDYIQVC---DSDTVLDPACTIEMLRVLEEDPQVGGVGGDVQILNKYDSWISFLSSVRYWMAFNVE 271
Cdd:pfam03142 185 yelFHQIwnvtGVSPDFYEYVlmvDADTKVFPDSLTRMVACMVDDPEIMGLCGETKIANKRQSWVTAIQVFEYYISHHLS 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 272 RACQSYFGCVQCISGPLGMYR-----------------NSLLQQFLE---DWYHQKFLgskCSFGDDRHLTNRVLSL--G 329
Cdd:pfam03142 265 KAFESVFGGVTCLPGCFSMYRikapkggdgywvpilasPDIVEHYSEnvvDTLHKKNL---LLLGEDRYLTTLMLKTfpK 341
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1061975058 330 YRTKYTARSKCLTETPTRYLRWLNQQTRWSKS 361
Cdd:pfam03142 342 RKTVFVPQAVCKTIAPDTFKVLLSQRRRWINS 373
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
187-361 2.68e-15

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


Pssm-ID: 133033 [Multi-domain]  Cd Length: 244  Bit Score: 75.81  E-value: 2.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 187 IMQKWGGKR--EVMYtaFKALGNSV-----DYIQVCDSDTVLDPACTIEMLRVLEEDPQVGGVGGDVQILNKYDSWISFL 259
Cdd:cd04190    47 AIKKNRGKRdsQLWF--FNYFCRVLfpddpEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQGPLVMY 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 260 SSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLEDWYHQKFLGSKCS------------FGDDRHLTNRVLS 327
Cdd:cd04190   125 QVFEYAISHWLDKAFESVFGFVTCLPGCFSMYRIEALKGDNGGKGPLLDYAYLTNtvdslhkknnldLGEDRILCTLLLK 204
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1061975058 328 LGYRTKYT--ARSKCLTETPTRYLRWLNQQTRWSKS 361
Cdd:cd04190   205 AGPKRKYLyvPGAVAETDVPETFVELLSQRRRWINS 240
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
85-346 2.84e-08

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 54.90  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058  85 PRSVALCIAAYQEDpEYLRKCLRSAQRIAFPN--LKVVMVVDGNrQEDTYmldifhEVLGGTEQAGFFVWRsnfHEAGEG 162
Cdd:cd06439    28 LPTVTIIIPAYNEE-AVIEAKLENLLALDYPRdrLEIIVVSDGS-TDGTA------EIAREYADKGVKLLR---FPERRG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 163 ETeASLQEGMERVRAvvwastfscimqkwggkrevmytafkalgnsvDYIQVCDSDTVLDPACTIEMLRVLEeDPQVGGV 242
Cdd:cd06439    97 KA-AALNRALALATG--------------------------------EIVVFTDANALLDPDALRLLVRHFA-DPSVGAV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 243 GGDVQILN------------KYDSWIsflssvrywmafnveRACQSYFGCVQCISGPLGMYRNSLLQQFLEDwyhqkflg 310
Cdd:cd06439   143 SGELVIVDgggsgsgeglywKYENWL---------------KRAESRLGSTVGANGAIYAIRRELFRPLPAD-------- 199
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1061975058 311 skcSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPT 346
Cdd:cd06439   200 ---TINDDFVLPLRIARQGYRVVYEPDAVAYEEVAE 232
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
88-334 4.35e-08

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 53.55  E-value: 4.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058  88 VALCIAAYQEdPEYLRKCLRSAQRIAFPNLKVVmVVDGNRQEDTymldifHEVLggteqagffvwrsnfheagegeteAS 167
Cdd:COG0463     4 VSVVIPTYNE-EEYLEEALESLLAQTYPDFEII-VVDDGSTDGT------AEIL------------------------RE 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 168 LQEGMERVRAVVwastfsciMQKWGGKREVMYTAFKALGNsvDYIQVCDSDTVLDPACTIEMLRVLEEDPqVGGVGGDVQ 247
Cdd:COG0463    52 LAAKDPRIRVIR--------LERNRGKGAARNAGLAAARG--DYIAFLDADDQLDPEKLEELVAALEEGP-ADLVYGSRL 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 248 ILNKYDSWISFLSSVRYWMAFnveracqsyFGCVQCISGPLGMYRNSLLQQfledwyhqkfLGSKCSFGDDRHLTnRVLS 327
Cdd:COG0463   121 IREGESDLRRLGSRLFNLVRL---------LTNLPDSTSGFRLFRREVLEE----------LGFDEGFLEDTELL-RALR 180

                  ....*..
gi 1061975058 328 LGYRTKY 334
Cdd:COG0463   181 HGFRIAE 187
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
86-364 8.18e-08

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


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 53.34  E-value: 8.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058  86 RSVALCIAAYQEDPEYLRKCLRSAQRIAFPNLKVVMVV--DGNRQEdtymLDIFHEVLGGTEQAGFFVWRSNFH-EAGeg 162
Cdd:cd06421     1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYPHDKLRVYVldDGRRPE----LRALAAELGVEYGYRYLTRPDNRHaKAG-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 163 eteaSLQEGMERVRAvvwastfscimqkwggkrevmytafkalgnsvDYIQVCDSDTVLDPACTIEMLRVLEEDPQVGGv 242
Cdd:cd06421    75 ----NLNNALAHTTG--------------------------------DFVAILDADHVPTPDFLRRTLGYFLDDPKVAL- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 243 ggdVQILNKYD-----SWIsFLSSVRYW-MAFNVERACQSYFGCVQCI-SGPLgmYRNSLLQQ---FLEDwyhqkflgsk 312
Cdd:cd06421   118 ---VQTPQFFYnpdpfDWL-ADGAPNEQeLFYGVIQPGRDRWGAAFCCgSGAV--VRREALDEiggFPTD---------- 181
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1061975058 313 cSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTRYLRWLNQQTRWSKSYFR 364
Cdd:cd06421   182 -SVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQ 232
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
211-420 1.22e-04

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


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 43.09  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 211 YIQVCDSDTVLDPACTIEMLRVLEeDPQVGGVGGDVQILNkYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGM 290
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMA-SPEVAIIQGPILPMN-VGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061975058 291 YRNSLLQQfLEDWyhqkflgSKCSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTRYLRWLNQQTRWSKSYFrewlyNS 370
Cdd:pfam13632  79 LRRSALQE-VGGW-------DDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCL-----LI 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1061975058 371 LWFHKHHLWMTYesvVTGFFPFFLIATVIQLFyRGRIWNILLFLLTVQLV 420
Cdd:pfam13632 146 LLIRLLGYLGTL---LWSGLPLALLLLLLFSI-SSLALVLLLLALLAGLL 191
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
324-367 3.91e-03

CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, Glucan Biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of glucan.


Pssm-ID: 133049 [Multi-domain]  Cd Length: 241  Bit Score: 39.16  E-value: 3.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1061975058 324 RVLSLGYRTKyTARSKCLTETPTRYLRWLNQQTRWSKSYFREWL 367
Cdd:cd06427   193 RLARAGYRTG-VLNSTTLEEANNALGNWIRQRSRWIKGYMQTWL 235
Glucan_BSP_MdoH cd04191
Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic ...
206-240 4.65e-03

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


Pssm-ID: 133034 [Multi-domain]  Cd Length: 254  Bit Score: 39.18  E-value: 4.65e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1061975058 206 GNSVDYIQVCDSDTVLDPACTIEMLRVLEEDPQVG 240
Cdd:cd04191    93 GSRYDYMVVLDADSLMSGDTIVRLVRRMEANPRAG 127
 
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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