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Conserved domains on  [gi|10441760|gb|AAG17180|]
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hyaluronan synthase 2 [Danio rerio]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10157701)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
84-361 3.89e-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: 292.24  E-value: 3.89e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760  84 SLALCIAAYQEDPNYLRKCLISVKRLTypGIKVIMVIDGNNDDDCYMMEifreimgrdkaatyiwksnyhhrgpeetees 163
Cdd:cd06434   1 DVTVIIPVYDEDPDVFRECLRSILRQK--PLEIIVVTDGDDEPYLSILS------------------------------- 47
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 164 yatslqhvsHLVLNNKCVCIMQKWGGKREVMYTAFKALgrSVDYVQVCDSDTMLDPASSVEMVKVLEeDPNVGGVGGDVQ 243
Cdd:cd06434  48 ---------QTVKYGGIFVITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQR 115
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 244 ILNKYESWVSFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFLEDWY--DQTFMGSHCSFGDDRHLTNRV 321
Cdd:cd06434 116 ILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEftNETFMGRRLNAGDDRFLTRYV 195
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 10441760 322 LSLGYATKYTARSKCLTETPITYLRWLNQQTRWSKSYFRE 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 3.89e-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: 292.24  E-value: 3.89e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760  84 SLALCIAAYQEDPNYLRKCLISVKRLTypGIKVIMVIDGNNDDDCYMMEifreimgrdkaatyiwksnyhhrgpeetees 163
Cdd:cd06434   1 DVTVIIPVYDEDPDVFRECLRSILRQK--PLEIIVVTDGDDEPYLSILS------------------------------- 47
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 164 yatslqhvsHLVLNNKCVCIMQKWGGKREVMYTAFKALgrSVDYVQVCDSDTMLDPASSVEMVKVLEeDPNVGGVGGDVQ 243
Cdd:cd06434  48 ---------QTVKYGGIFVITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQR 115
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 244 ILNKYESWVSFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFLEDWY--DQTFMGSHCSFGDDRHLTNRV 321
Cdd:cd06434 116 ILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEftNETFMGRRLNAGDDRFLTRYV 195
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 10441760 322 LSLGYATKYTARSKCLTETPITYLRWLNQQTRWSKSYFRE 361
Cdd:cd06434 196 LSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSNWRS 235
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
48-468 7.41e-20

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: 90.19  E-value: 7.41e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760  48 LYGAILVIHLIIQSVFALLEHRNMKRSLetpiklnKSLALCIAAYQEDPNyLRKCLISVKRLTYPGIKV-IMVIDGNNDD 126
Cdd:COG1215   1 LLLLLALLALLYLLLLALARRRRAPADL-------PRVSVIIPAYNEEAV-IEETLRSLLAQDYPKEKLeVIVVDDGSTD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 127 DCYmmEIFREIMGRDKAATYIwksnyhHRGPEeteesyatslqhvshlvlnnkcvcimqkwGGKREVMYTAFKAlgRSVD 206
Cdd:COG1215  73 ETA--EIARELAAEYPRVRVI------ERPEN-----------------------------GGKAAALNAGLKA--ARGD 113
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 207 YVQVCDSDTMLDPASSVEMVKVLEeDPNVGgvggdvqilnkyeswvsflssvrywmafnieracqsyfgcvqcISGPLGM 286
Cdd:COG1215 114 IVVFLDADTVLDPDWLRRLVAAFA-DPGVG-------------------------------------------ASGANLA 149
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 287 YRNSLLHEFleDWYDqtfmgsHCSFGDDRHLTNRVLSLGYATKYTARSKCLTETPITYLRWLNQQTRWSKSYFREWLYNS 366
Cdd:COG1215 150 FRREALEEV--GGFD------EDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHR 221
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 367 LWFHKHHLWmtyeavitgFFPFFLIATAIQLFYQGRIWNILLFLLIVQVVALIKssfasclrgniVMVFMSFYSVLYMSS 446
Cdd:COG1215 222 PLLRPRRLL---------LFLLLLLLPLLLLLLLLALLALLLLLLPALLLALLL-----------ALRRRRLLLPLLHLL 281
                       410       420
                ....*....|....*....|..
gi 10441760 447 LLPAKMFAIATINKSGWGTSGR 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 1.51e-14

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


Pssm-ID: 367353 [Multi-domain]  Cd Length: 527  Bit Score: 76.34  E-value: 1.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760   206 DYVQVCDSDTMLDPASSVEMVKVLEEDPNVGGVGGDVQILNKYESWVSFLSSVRYWMAFNIERACQSYFGCVQCISGPLG 285
Cdd:pfam03142 203 EYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGETKIANKRQSWVTAIQVFEYYISHHLSKAFESVFGGVTCLPGCFS 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760   286 MYR-----------------NSLLHEFLEDWYDQTFMGSHCSFGDDRHLTNRVLSL--GYATKYTARSKCLTETPITYLR 346
Cdd:pfam03142 283 MYRikapkggdgywvpilasPDIVEHYSENVVDTLHKKNLLLLGEDRYLTTLMLKTfpKRKTVFVPQAVCKTIAPDTFKV 362
                         170
                  ....*....|.
gi 10441760   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 3.89e-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: 292.24  E-value: 3.89e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760  84 SLALCIAAYQEDPNYLRKCLISVKRLTypGIKVIMVIDGNNDDDCYMMEifreimgrdkaatyiwksnyhhrgpeetees 163
Cdd:cd06434   1 DVTVIIPVYDEDPDVFRECLRSILRQK--PLEIIVVTDGDDEPYLSILS------------------------------- 47
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 164 yatslqhvsHLVLNNKCVCIMQKWGGKREVMYTAFKALgrSVDYVQVCDSDTMLDPASSVEMVKVLEeDPNVGGVGGDVQ 243
Cdd:cd06434  48 ---------QTVKYGGIFVITVPHPGKRRALAEGIRHV--TTDIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQR 115
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 244 ILNKYESWVSFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFLEDWY--DQTFMGSHCSFGDDRHLTNRV 321
Cdd:cd06434 116 ILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAYRTEILKDFLFLEEftNETFMGRRLNAGDDRFLTRYV 195
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 10441760 322 LSLGYATKYTARSKCLTETPITYLRWLNQQTRWSKSYFRE 361
Cdd:cd06434 196 LSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSNWRS 235
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
89-294 2.49e-25

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: 102.69  E-value: 2.49e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760  89 IAAYQEDPNyLRKCLISVKRLTYPGIKVIMVIDGNNDDdcymmeiFREIMgRDKAATYIWKSNYHHRGPEeteesyatsl 168
Cdd:cd06423   3 VPAYNEEAV-IERTIESLLALDYPKLEVIVVDDGSTDD-------TLEIL-EELAALYIRRVLVVRDKEN---------- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 169 qhvshlvlnnkcvcimqkwGGKREVMYTAFKALgrSVDYVQVCDSDTMLDPASSVEMVKVLEEDPNVGGVGGDVQILNKY 248
Cdd:cd06423  64 -------------------GGKAGALNAGLRHA--KGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGS 122
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 10441760 249 ESWVSFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHE 294
Cdd:cd06423 123 ENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAFGAFRREALRE 168
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
48-468 7.41e-20

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: 90.19  E-value: 7.41e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760  48 LYGAILVIHLIIQSVFALLEHRNMKRSLetpiklnKSLALCIAAYQEDPNyLRKCLISVKRLTYPGIKV-IMVIDGNNDD 126
Cdd:COG1215   1 LLLLLALLALLYLLLLALARRRRAPADL-------PRVSVIIPAYNEEAV-IEETLRSLLAQDYPKEKLeVIVVDDGSTD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 127 DCYmmEIFREIMGRDKAATYIwksnyhHRGPEeteesyatslqhvshlvlnnkcvcimqkwGGKREVMYTAFKAlgRSVD 206
Cdd:COG1215  73 ETA--EIARELAAEYPRVRVI------ERPEN-----------------------------GGKAAALNAGLKA--ARGD 113
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 207 YVQVCDSDTMLDPASSVEMVKVLEeDPNVGgvggdvqilnkyeswvsflssvrywmafnieracqsyfgcvqcISGPLGM 286
Cdd:COG1215 114 IVVFLDADTVLDPDWLRRLVAAFA-DPGVG-------------------------------------------ASGANLA 149
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 287 YRNSLLHEFleDWYDqtfmgsHCSFGDDRHLTNRVLSLGYATKYTARSKCLTETPITYLRWLNQQTRWSKSYFREWLYNS 366
Cdd:COG1215 150 FRREALEEV--GGFD------EDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHR 221
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 367 LWFHKHHLWmtyeavitgFFPFFLIATAIQLFYQGRIWNILLFLLIVQVVALIKssfasclrgniVMVFMSFYSVLYMSS 446
Cdd:COG1215 222 PLLRPRRLL---------LFLLLLLLPLLLLLLLLALLALLLLLLPALLLALLL-----------ALRRRRLLLPLLHLL 281
                       410       420
                ....*....|....*....|..
gi 10441760 447 LLPAKMFAIATINKSGWGTSGR 468
Cdd:COG1215 282 YGLLLLLAALRGKKVVWKKTPR 303
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
159-357 9.93e-18

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: 82.74  E-value: 9.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 159 ETEESYATSLQHVSHLVLN----------NKCVCI-----MQKWGGKR--EVMYtaFKALGRSV-----DYVQVCDSDTM 216
Cdd:cd04190   8 EDEEELARTLDSILKNDYPfcarggdswkKIVVCVifdgaIKKNRGKRdsQLWF--FNYFCRVLfpddpEFILLVDADTK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 217 LDPASSVEMVKVLEEDPNVGGVGGDVQILNKYESWVSFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFL 296
Cdd:cd04190  86 FDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQGPLVMYQVFEYAISHWLDKAFESVFGFVTCLPGCFSMYRIEALKGDN 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10441760 297 EDWYDQTFMGSHCS------------FGDDRHLTNRVLSLGYATKYT--ARSKCLTETPITYLRWLNQQTRWSKS 357
Cdd:cd04190 166 GGKGPLLDYAYLTNtvdslhkknnldLGEDRILCTLLLKAGPKRKYLyvPGAVAETDVPETFVELLSQRRRWINS 240
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
206-357 1.51e-14

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


Pssm-ID: 367353 [Multi-domain]  Cd Length: 527  Bit Score: 76.34  E-value: 1.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760   206 DYVQVCDSDTMLDPASSVEMVKVLEEDPNVGGVGGDVQILNKYESWVSFLSSVRYWMAFNIERACQSYFGCVQCISGPLG 285
Cdd:pfam03142 203 EYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGETKIANKRQSWVTAIQVFEYYISHHLSKAFESVFGGVTCLPGCFS 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760   286 MYR-----------------NSLLHEFLEDWYDQTFMGSHCSFGDDRHLTNRVLSL--GYATKYTARSKCLTETPITYLR 346
Cdd:pfam03142 283 MYRikapkggdgywvpilasPDIVEHYSENVVDTLHKKNLLLLGEDRYLTTLMLKTfpKRKTVFVPQAVCKTIAPDTFKV 362
                         170
                  ....*....|.
gi 10441760   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 ...
85-355 2.03e-11

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: 63.93  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760    85 LALCIAAYQEDPnYLRKCLISVKRLTYPGIKVIMVIDGNNDDDCymmEIFREIMGRDKAATYIWKSNYHHRGPeeteesy 164
Cdd:pfam13641   4 VSVVVPAFNEDS-VLGRVLEAILAQPYPPVEVVVVVNPSDAETL---DVAEEIAARFPDVRLRVIRNARLLGP------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760   165 atslqhvshlvlnnkcvcimqkwGGKREVMYTAFKALGRsvDYVQVCDSDTMLDPASSVEMVKVLEeDPNVGGVGGDVQI 244
Cdd:pfam13641  73 -----------------------TGKSRGLNHGFRAVKS--DLVVLHDDDSVLHPGTLKKYVQYFD-SPKVGAVGTPVFS 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760   245 LNKyESWVSFLSSVRYWMAFnIERACQSYFGCVQCISGPLGMYRNSLLHEFLedwydqTFMGSHCsFGDDRHLTNRVLSL 324
Cdd:pfam13641 127 LNR-STMLSALGALEFALRH-LRMMSLRLALGVLPLSGAGSAIRREVLKELG------LFDPFFL-LGDDKSLGRRLRRH 197
                         250       260       270
                  ....*....|....*....|....*....|.
gi 10441760   325 GYATKYTARSKCLTETPITYLRWLNQQTRWS 355
Cdd:pfam13641 198 GWRVAYAPDAAVRTVFPTYLAASIKQRARWV 228
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
82-299 2.04e-08

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 54.71  E-value: 2.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760  82 NKSLALCIAAYQEdPNYLRKCLISVKRLTYPGIKVImVIDGNNDDDCymMEIFREIMGRDKAATYIwksnyHHrgpeete 161
Cdd:COG0463   1 MPLVSVVIPTYNE-EEYLEEALESLLAQTYPDFEII-VVDDGSTDGT--AEILRELAAKDPRIRVI-----RL------- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 162 esyatslqhvshlvlnnkcvcimQKWGGKREVMYTAFK-ALGrsvDYVQVCDSDTMLDPASSVEMVKVLEEDPnVGGVGG 240
Cdd:COG0463  65 -----------------------ERNRGKGAARNAGLAaARG---DYIAFLDADDQLDPEKLEELVAALEEGP-ADLVYG 117
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 10441760 241 DVQILNKYESWVSFLSSVRYWMAFnieracqsyFGCVQCISGPLGMYRNSLLHE------FLEDW 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 4.33e-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: 51.43  E-value: 4.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760  84 SLALCIAAYQEDPNYLRKcLISVKRLTYPG--IKVIMVIDGNNDDdcymmeifreimgrdkaatyiwksnyhhrgpeeTE 161
Cdd:cd06439  30 TVTIIIPAYNEEAVIEAK-LENLLALDYPRdrLEIIVVSDGSTDG---------------------------------TA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 162 ESYATSLQHVSHLVLN--NKcvcimqkwgGKREVMYTAFKALgrSVDYVQVCDSDTMLDPASSVEMVKVLEeDPNVGGVG 239
Cdd:cd06439  76 EIAREYADKGVKLLRFpeRR---------GKAAALNRALALA--TGEIVVFTDANALLDPDALRLLVRHFA-DPSVGAVS 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 240 GDVQILN------------KYESWVsflssvrywmafnieRACQSYFGCVQCISGPLGMYRNSLLHEFLEDwydqtfmgs 307
Cdd:cd06439 144 GELVIVDgggsgsgeglywKYENWL---------------KRAESRLGSTVGANGAIYAIRRELFRPLPAD--------- 199
                       250       260       270
                ....*....|....*....|....*....|....
gi 10441760 308 hcSFGDDRHLTNRVLSLGYATKYTARSKCLTETP 341
Cdd:cd06439 200 --TINDDFVLPLRIARQGYRVVYEPDAVAYEEVA 231
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
84-360 4.66e-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: 47.95  E-value: 4.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760  84 SLALCIAAYQEDPNYLRKCLISVKRLTYPGIKV-IMVIDGNNDDDcymMEIFREIMGRDKAATYIWKSNYHHR--GPeet 160
Cdd:cd06421   2 TVDVFIPTYNEPLEIVRKTLRAALAIDYPHDKLrVYVLDDGRRPE---LRALAAELGVEYGYRYLTRPDNRHAkaGN--- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 161 eesyatslqhvshlvLNNkcvcimqkwggkrevmytafkALGRS-VDYVQVCDSDTMLDPASSVEMVKVLEEDPNVGGVG 239
Cdd:cd06421  76 ---------------LNN---------------------ALAHTtGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQ 119
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760 240 GdVQIlnkyeswvsflssvrYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFledwydqtFMGSHC---------- 309
Cdd:cd06421 120 T-PQF---------------FYNPDPFDWLADGAPNEQELFYGVIQPGRDRWGAAF--------CCGSGAvvrrealdei 175
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 10441760 310 ------SFGDDRHLTNRVLSLGYATKYTARSKCLTETPITYLRWLNQQTRWSKSYFR 360
Cdd:cd06421 176 ggfptdSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQ 232
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
87-294 3.87e-03

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: 38.53  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760    87 LCIAAYQEdPNYLRKCLISVKRLTYPGIKVIMVIDGNNDDdcymmeiFREIMgrdkaatyiwksnyhhrgpeeteESYAT 166
Cdd:pfam00535   2 VIIPTYNE-EKYLLETLESLLNQTYPNFEIIVVDDGSTDG-------TVEIA-----------------------EEYAK 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760   167 SLQHVSHLVLNNKcvcimqkwGGKREVMYTAFK-ALGrsvDYVQVCDSDTMLDPASSVEMVKVLEEDPnVGGVGGDVQIL 245
Cdd:pfam00535  51 KDPRVRVIRLPEN--------RGKAGARNAGLRaATG---DYIAFLDADDEVPPDWLEKLVEALEEDG-ADVVVGSRYVI 118
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 10441760   246 NKYESWVSFLSSVRYWMAFNIERACQSYFGcVQCISGPLGMYRNSLLHE 294
Cdd:pfam00535 119 FGETGEYRRASRITLSRLPFFLGLRLLGLN-LPFLIGGFALYRREALEE 166
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
212-416 4.57e-03

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: 38.47  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760   212 DSDTMLDPASsVEMVKVLEEDPNVGGVGGDVQILNkyesWVSFLSSV-RYWMAFNIERAC--QSYFGCVQCISGplgmyR 288
Cdd:pfam13632   6 DADTVLPPDC-LLGIANEMASPEVAIIQGPILPMN----VGNYLEELaALFFADDHGKSIpvRMALGRVLPFVG-----S 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441760   289 NSLLHefLEDWYD-QTFMGSHcsFGDDRHLTNRVLSLGYATKYTARSKCLTETPITYLRWLNQQTRWSKSYFrewlyNSL 367
Cdd:pfam13632  76 GAFLR--RSALQEvGGWDDGS--VSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCL-----LIL 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 10441760   368 WFHKHHLWMTYeavITGFFPFFLIATAIQLFYqGRIWNILLFLLIVQVV 416
Cdd:pfam13632 147 LIRLLGYLGTL---LWSGLPLALLLLLLFSIS-SLALVLLLLALLAGLL 191
 
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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