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Conserved domains on  [gi|148887356|sp|O13353|]
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RecName: Full=Chitin synthase 4; AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 4; AltName: Full=Class-IV chitin synthase 4

Protein Classification

chitin synthase( domain architecture ID 12042369)

chitin synthase converts UDP-N-acetyl-D-glucosamine into chitin and UDP; chitin is a structural polymer of the cell wall and septum

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
659-1184 0e+00

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: 1033.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   659 PSGFIHDSVVPQPPSDWMPFGFPLAHTICLVTAYSEGELGLRTTLDSVAMTDYPNSHKVILVICDGIIKGKGESKSTPEY 738
Cdd:pfam03142    1 VSTIIHKFIAAQPLGTKRPFGFPLKHTICLVTCYSEGEEGLRTTLDSLATTDYPDSHKLLLVICDGMIKGSGNDRSTPDI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   739 VLDMMKDHTIPVEDVEAFSYVAVASGSKRHNMAKIYAGFYDYGTQSNIPLDKQQRVPMMVVVKCGTPDEMVKSKPGNRGK 818
Cdd:pfam03142   81 VLDMMKDAVIPKEDPEPLSYVAVASGSKRHNMAKVYAGFYEYDGDSHIPEEKQQRVPMIVVVKCGTPSEASEKKPGNRGK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   819 RDSQIILMSFLQKVMFDERMTELEYEMFNGLWKVTGISPDFYEIVLMVDADTKVFPDSLTHMISAMVKDPEIMGLCGETK 898
Cdd:pfam03142  161 RDSQIILMRFLQKVHFDERMTPLEYELFHQIWNVTGVSPDFYEYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGETK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   899 IANKRDSWVSAIQVFEYFISHHLAKSFESVFGGVTCLPGCFCMYRIKAPKGAQNYWVPILANPDVVEHYSENVVDTLHKK 978
Cdd:pfam03142  241 IANKRQSWVTAIQVFEYYISHHLSKAFESVFGGVTCLPGCFSMYRIKAPKGGDGYWVPILASPDIVEHYSENVVDTLHKK 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   979 NLLLLGEDRYLTTLMLRTFPKRKQVFVPQAVCKTTVPDSFMVLLSQRRRWINSTIHNLMELVLVRDLCGTFCFSMQFVIF 1058
Cdd:pfam03142  321 NLLLLGEDRYLTTLMLKTFPKRKTVFVPQAVCKTIAPDTFKVLLSQRRRWINSTVHNLMELVLVRDLCGTFCFSMQFVVF 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  1059 IELIGTLVLPAAIAFTFYVVIISII-NQPPQIIPLVLLGLILGLPAILIIITAHSWSYVLWMLIYLLSLPVWNFVLPAYA 1137
Cdd:pfam03142  401 IELIGTVVLPAAIAFTVYLIVISILtPDPVPVIPLVLLAAILGLPAILILLTTRKWVYIGWMLVYLLALPIWNFVLPLYA 480
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 148887356  1138 FWKFDDFSWGDTRKTAGEKTKKAGIEYEGEFDSSKITMKRWAEFERD 1184
Cdd:pfam03142  481 FWHFDDFSWGNTRVVAGEKGKKVHGTDEGEFDPSKIPMKRWEEFERE 527
 
Name Accession Description Interval E-value
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
659-1184 0e+00

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: 1033.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   659 PSGFIHDSVVPQPPSDWMPFGFPLAHTICLVTAYSEGELGLRTTLDSVAMTDYPNSHKVILVICDGIIKGKGESKSTPEY 738
Cdd:pfam03142    1 VSTIIHKFIAAQPLGTKRPFGFPLKHTICLVTCYSEGEEGLRTTLDSLATTDYPDSHKLLLVICDGMIKGSGNDRSTPDI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   739 VLDMMKDHTIPVEDVEAFSYVAVASGSKRHNMAKIYAGFYDYGTQSNIPLDKQQRVPMMVVVKCGTPDEMVKSKPGNRGK 818
Cdd:pfam03142   81 VLDMMKDAVIPKEDPEPLSYVAVASGSKRHNMAKVYAGFYEYDGDSHIPEEKQQRVPMIVVVKCGTPSEASEKKPGNRGK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   819 RDSQIILMSFLQKVMFDERMTELEYEMFNGLWKVTGISPDFYEIVLMVDADTKVFPDSLTHMISAMVKDPEIMGLCGETK 898
Cdd:pfam03142  161 RDSQIILMRFLQKVHFDERMTPLEYELFHQIWNVTGVSPDFYEYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGETK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   899 IANKRDSWVSAIQVFEYFISHHLAKSFESVFGGVTCLPGCFCMYRIKAPKGAQNYWVPILANPDVVEHYSENVVDTLHKK 978
Cdd:pfam03142  241 IANKRQSWVTAIQVFEYYISHHLSKAFESVFGGVTCLPGCFSMYRIKAPKGGDGYWVPILASPDIVEHYSENVVDTLHKK 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   979 NLLLLGEDRYLTTLMLRTFPKRKQVFVPQAVCKTTVPDSFMVLLSQRRRWINSTIHNLMELVLVRDLCGTFCFSMQFVIF 1058
Cdd:pfam03142  321 NLLLLGEDRYLTTLMLKTFPKRKTVFVPQAVCKTIAPDTFKVLLSQRRRWINSTVHNLMELVLVRDLCGTFCFSMQFVVF 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  1059 IELIGTLVLPAAIAFTFYVVIISII-NQPPQIIPLVLLGLILGLPAILIIITAHSWSYVLWMLIYLLSLPVWNFVLPAYA 1137
Cdd:pfam03142  401 IELIGTVVLPAAIAFTVYLIVISILtPDPVPVIPLVLLAAILGLPAILILLTTRKWVYIGWMLVYLLALPIWNFVLPLYA 480
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 148887356  1138 FWKFDDFSWGDTRKTAGEKTKKAGIEYEGEFDSSKITMKRWAEFERD 1184
Cdd:pfam03142  481 FWHFDDFSWGNTRVVAGEKGKKVHGTDEGEFDPSKIPMKRWEEFERE 527
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
687-1035 4.84e-103

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: 325.80  E-value: 4.84e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  687 CLVTAYSEGELGLRTTLDSVAMTDYP--------NSHKVILVICDGIIKGkgeskstpeyvldmmkdhtipvedveafsy 758
Cdd:cd04190     1 VCVTMYNEDEEELARTLDSILKNDYPfcarggdsWKKIVVCVIFDGAIKK------------------------------ 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  759 vavasgskrhnmakiyagfydygtqsnipldkqqrvpmmvvvkcgtpdemvkskpgNRGKRDSQIILMSFLQKVMFderm 838
Cdd:cd04190    51 --------------------------------------------------------NRGKRDSQLWFFNYFCRVLF---- 70
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  839 teleyemfnglwkvtgisPDFYEIVLMVDADTKVFPDSLTHMISAMVKDPEIMGLCGETKIANKRDSWVSAIQVFEYFIS 918
Cdd:cd04190    71 ------------------PDDPEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQGPLVMYQVFEYAIS 132
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  919 HHLAKSFESVFGGVTCLPGCFCMYRIKAPKGAQNYWVPILANpdvveHYSENVVDTLHKKNLLLLGEDRYLTTLMLRTFP 998
Cdd:cd04190   133 HWLDKAFESVFGFVTCLPGCFSMYRIEALKGDNGGKGPLLDY-----AYLTNTVDSLHKKNNLDLGEDRILCTLLLKAGP 207
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 148887356  999 KRKQVFVPQAVCKTTVPDSFMVLLSQRRRWINSTIHN 1035
Cdd:cd04190   208 KRKYLYVPGAVAETDVPETFVELLSQRRRWINSTIAN 244
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
860-1151 9.09e-11

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: 64.38  E-value: 9.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  860 YEIVLMVDADTKVFPDSLTHMISAMvKDPEImglcgetkiankrdswvsaiqvfeyfishhlaksfesvfggvtCLPGCF 939
Cdd:COG1215   112 GDIVVFLDADTVLDPDWLRRLVAAF-ADPGV-------------------------------------------GASGAN 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  940 CMYRIKApkgaqnywvpILAnpdvVEHYSENVvdtlhkknlllLGEDRYLTTLMLRTfpKRKQVFVPQAVCKTTVPDSFM 1019
Cdd:COG1215   148 LAFRREA----------LEE----VGGFDEDT-----------LGEDLDLSLRLLRA--GYRIVYVPDAVVYEEAPETLR 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356 1020 VLLSQRRRWINSTIHNLMELVLVRDLCGTFCFSMQFVIFIeLIGTLVLPAAIAFTFYVVIISIinqppqiiplvllglil 1099
Cdd:COG1215   201 ALFRQRRRWARGGLQLLLKHRPLLRPRRLLLFLLLLLLPL-LLLLLLLALLALLLLLLPALLL----------------- 262
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 148887356 1100 glpAILIIITAHSWSYVLWMLIYllslpvwnFVLPAYAFWKFDDFSWGDTRK 1151
Cdd:COG1215   263 ---ALLLALRRRRLLLPLLHLLY--------GLLLLLAALRGKKVVWKKTPR 303
 
Name Accession Description Interval E-value
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
659-1184 0e+00

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: 1033.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   659 PSGFIHDSVVPQPPSDWMPFGFPLAHTICLVTAYSEGELGLRTTLDSVAMTDYPNSHKVILVICDGIIKGKGESKSTPEY 738
Cdd:pfam03142    1 VSTIIHKFIAAQPLGTKRPFGFPLKHTICLVTCYSEGEEGLRTTLDSLATTDYPDSHKLLLVICDGMIKGSGNDRSTPDI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   739 VLDMMKDHTIPVEDVEAFSYVAVASGSKRHNMAKIYAGFYDYGTQSNIPLDKQQRVPMMVVVKCGTPDEMVKSKPGNRGK 818
Cdd:pfam03142   81 VLDMMKDAVIPKEDPEPLSYVAVASGSKRHNMAKVYAGFYEYDGDSHIPEEKQQRVPMIVVVKCGTPSEASEKKPGNRGK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   819 RDSQIILMSFLQKVMFDERMTELEYEMFNGLWKVTGISPDFYEIVLMVDADTKVFPDSLTHMISAMVKDPEIMGLCGETK 898
Cdd:pfam03142  161 RDSQIILMRFLQKVHFDERMTPLEYELFHQIWNVTGVSPDFYEYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGETK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   899 IANKRDSWVSAIQVFEYFISHHLAKSFESVFGGVTCLPGCFCMYRIKAPKGAQNYWVPILANPDVVEHYSENVVDTLHKK 978
Cdd:pfam03142  241 IANKRQSWVTAIQVFEYYISHHLSKAFESVFGGVTCLPGCFSMYRIKAPKGGDGYWVPILASPDIVEHYSENVVDTLHKK 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   979 NLLLLGEDRYLTTLMLRTFPKRKQVFVPQAVCKTTVPDSFMVLLSQRRRWINSTIHNLMELVLVRDLCGTFCFSMQFVIF 1058
Cdd:pfam03142  321 NLLLLGEDRYLTTLMLKTFPKRKTVFVPQAVCKTIAPDTFKVLLSQRRRWINSTVHNLMELVLVRDLCGTFCFSMQFVVF 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  1059 IELIGTLVLPAAIAFTFYVVIISII-NQPPQIIPLVLLGLILGLPAILIIITAHSWSYVLWMLIYLLSLPVWNFVLPAYA 1137
Cdd:pfam03142  401 IELIGTVVLPAAIAFTVYLIVISILtPDPVPVIPLVLLAAILGLPAILILLTTRKWVYIGWMLVYLLALPIWNFVLPLYA 480
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 148887356  1138 FWKFDDFSWGDTRKTAGEKTKKAGIEYEGEFDSSKITMKRWAEFERD 1184
Cdd:pfam03142  481 FWHFDDFSWGNTRVVAGEKGKKVHGTDEGEFDPSKIPMKRWEEFERE 527
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
687-1035 4.84e-103

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: 325.80  E-value: 4.84e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  687 CLVTAYSEGELGLRTTLDSVAMTDYP--------NSHKVILVICDGIIKGkgeskstpeyvldmmkdhtipvedveafsy 758
Cdd:cd04190     1 VCVTMYNEDEEELARTLDSILKNDYPfcarggdsWKKIVVCVIFDGAIKK------------------------------ 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  759 vavasgskrhnmakiyagfydygtqsnipldkqqrvpmmvvvkcgtpdemvkskpgNRGKRDSQIILMSFLQKVMFderm 838
Cdd:cd04190    51 --------------------------------------------------------NRGKRDSQLWFFNYFCRVLF---- 70
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  839 teleyemfnglwkvtgisPDFYEIVLMVDADTKVFPDSLTHMISAMVKDPEIMGLCGETKIANKRDSWVSAIQVFEYFIS 918
Cdd:cd04190    71 ------------------PDDPEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQGPLVMYQVFEYAIS 132
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  919 HHLAKSFESVFGGVTCLPGCFCMYRIKAPKGAQNYWVPILANpdvveHYSENVVDTLHKKNLLLLGEDRYLTTLMLRTFP 998
Cdd:cd04190   133 HWLDKAFESVFGFVTCLPGCFSMYRIEALKGDNGGKGPLLDY-----AYLTNTVDSLHKKNNLDLGEDRILCTLLLKAGP 207
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 148887356  999 KRKQVFVPQAVCKTTVPDSFMVLLSQRRRWINSTIHN 1035
Cdd:cd04190   208 KRKYLYVPGAVAETDVPETFVELLSQRRRWINSTIAN 244
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
860-946 6.94e-21

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: 91.52  E-value: 6.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  860 YEIVLMVDADTKVFPDSLTHMISAMVKDPEIMGLCGETKIANKRDSWVSAIQVFEYFISHHLAKSFESVFGGVTCLPGCF 939
Cdd:cd06423    79 GDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAF 158

                  ....*..
gi 148887356  940 CMYRIKA 946
Cdd:cd06423   159 GAFRREA 165
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
861-1035 5.19e-11

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: 64.20  E-value: 5.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  861 EIVLMVDADTKVFPDSLTHMISAMVkDPEIMGLCGETKIANKRDSWVSAIQV-------FEYFISHhlaksfeSVFGGVT 933
Cdd:cd06434    79 DIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQRILRPRDSKWSFLAAeylerrnEEIRAAM-------SYDGGVP 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  934 CLPGCFCMYRIKapkgaqnywvpILANPDvvehYSENVVDTLHKKNLLLLGEDRYLTTLMLRTFpkRKQVFVPQAVCKTT 1013
Cdd:cd06434   151 CLSGRTAAYRTE-----------ILKDFL----FLEEFTNETFMGRRLNAGDDRFLTRYVLSHG--YKTVYQYTSEAYTE 213
                         170       180
                  ....*....|....*....|..
gi 148887356 1014 VPDSFMVLLSQRRRWINSTIHN 1035
Cdd:cd06434   214 TPENYKKFLKQQLRWSRSNWRS 235
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
860-1151 9.09e-11

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: 64.38  E-value: 9.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  860 YEIVLMVDADTKVFPDSLTHMISAMvKDPEImglcgetkiankrdswvsaiqvfeyfishhlaksfesvfggvtCLPGCF 939
Cdd:COG1215   112 GDIVVFLDADTVLDPDWLRRLVAAF-ADPGV-------------------------------------------GASGAN 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  940 CMYRIKApkgaqnywvpILAnpdvVEHYSENVvdtlhkknlllLGEDRYLTTLMLRTfpKRKQVFVPQAVCKTTVPDSFM 1019
Cdd:COG1215   148 LAFRREA----------LEE----VGGFDEDT-----------LGEDLDLSLRLLRA--GYRIVYVPDAVVYEEAPETLR 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356 1020 VLLSQRRRWINSTIHNLMELVLVRDLCGTFCFSMQFVIFIeLIGTLVLPAAIAFTFYVVIISIinqppqiiplvllglil 1099
Cdd:COG1215   201 ALFRQRRRWARGGLQLLLKHRPLLRPRRLLLFLLLLLLPL-LLLLLLLALLALLLLLLPALLL----------------- 262
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 148887356 1100 glpAILIIITAHSWSYVLWMLIYllslpvwnFVLPAYAFWKFDDFSWGDTRK 1151
Cdd:COG1215   263 ---ALLLALRRRRLLLPLLHLLY--------GLLLLLAALRGKKVVWKKTPR 303
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
862-1083 2.58e-10

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: 61.20  E-value: 2.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   862 IVLMVDADTKVFPDSLtHMISAMVKDPEIMGLCGETkIANKRDSWVSAIQVFEYFISHHLAKSFESVFGGVTCLPGCFCM 941
Cdd:pfam13632    1 WILLLDADTVLPPDCL-LGIANEMASPEVAIIQGPI-LPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   942 YRIKApkgaqnywvpilanpdvvehysenvVDTLHKKNLLLLGEDrylTTLMLRTFPKRKQV-FVPQAVCKTTVPDSFMV 1020
Cdd:pfam13632   79 LRRSA-------------------------LQEVGGWDDGSVSED---FDFGLRLQRAGYRVrFAPYSAVYEKSPLTFRD 130
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148887356  1021 LLSQRRRWINStIHNLMELVLVRDLCGTFCFSMQFVIFIELIGTLVLPAAIAFTFYVVIISII 1083
Cdd:pfam13632  131 FLRQRRRWAYG-CLLILLIRLLGYLGTLLWSGLPLALLLLLLFSISSLALVLLLLALLAGLLL 192
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
861-1031 3.32e-04

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: 43.51  E-value: 3.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   861 EIVLMVDADTKVFPDSLThMISAMVKDPEiMGLCGETKIANKRDSWVSAIQVFEYFIsHHLAKSFESVFGGVTCLPGCFC 940
Cdd:pfam13641   89 DLVVLHDDDSVLHPGTLK-KYVQYFDSPK-VGAVGTPVFSLNRSTMLSALGALEFAL-RHLRMMSLRLALGVLPLSGAGS 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356   941 MYRIkapkgaqnywvpilanpDVVEHYsenvvDTLHKknLLLLGEDrYLTTLMLRTFpKRKQVFVPQAVCKTTVPDSFMV 1020
Cdd:pfam13641  166 AIRR-----------------EVLKEL-----GLFDP--FFLLGDD-KSLGRRLRRH-GWRVAYAPDAAVRTVFPTYLAA 219
                          170
                   ....*....|.
gi 148887356  1021 LLSQRRRWINS 1031
Cdd:pfam13641  220 SIKQRARWVYG 230
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
840-921 4.28e-04

EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier.


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 42.59  E-value: 4.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148887356  840 ELEYeMFNGLWKVtgisPDFYEIVLMVDADTKVFPDSLTHMISAMVKDPEIMGLCGETKiaNKRDSWVSAIQVFEYFISH 919
Cdd:cd06438    67 ALDF-GFRHLLNL----ADDPDAVVVFDADNLVDPNALEELNARFAAGARVVQAYYNSK--NPDDSWITRLYAFAFLVFN 139

                  ..
gi 148887356  920 HL 921
Cdd:cd06438   140 RL 141
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
861-933 5.06e-04

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 42.37  E-value: 5.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148887356  861 EIVLMVDADTKVFPDSLTHmISAMVKDPEIMGLCGETKIANKRDSWVSAIQVFEYFISHHLAKSFESVFGGVT 933
Cdd:cd06436    91 VIIAVIDADGRLDPNALEA-VAPYFSDPRVAGTQSRVRMYNRHKNLLTILQDLEFFIIIAATQSLRALTGTVG 162
 
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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