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Conserved domains on  [gi|2130390345|gb|KAH7604547|]
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Chitin synthase [[Candida] glabrata]

Protein Classification

chitin synthase domain-containing protein( domain architecture ID 1002772)

chitin synthase domain-containing protein; chitin synthase is a membranous isoenzyme which catalyzes the multiple transfer of GlcNAc residues from UDPGlcNAc onto the nonreducing end of the growing chitin chain to biosynthesize chitin.

Gene Ontology:  GO:0004100

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Chitin_synth_2 super family cl37687
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
531-1048 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).


The actual alignment was detected with superfamily member pfam03142:

Pssm-ID: 367353 [Multi-domain]  Cd Length: 527  Bit Score: 703.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  531 IIHKNVVkPNNIIHGSSDGF--LNTICFVTCYSEGVRELRSTLDALCTTTYPNTHKLIILVCDGQVTGAHNKKLTSEIAL 608
Cdd:pfam03142    4 IIHKFIA-AQPLGTKRPFGFplKHTICLVTCYSEGEEGLRTTLDSLATTDYPDSHKLLLVICDGMIKGSGNDRSTPDIVL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  609 NMITDFIEDPNEVIPYSYLSIASGAKRFNMAKVYGGYYKYDSD-TVEESQQQQVPIVLVSKCGSFYEIhSSPKPGNRGKR 687
Cdd:pfam03142   83 DMMKDAVIPKEDPEPLSYVAVASGSKRHNMAKVYAGFYEYDGDsHIPEEKQQRVPMIVVVKCGTPSEA-SEKKPGNRGKR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  688 DSQIILMSLLQRAICNERMSELEFQLLKVIWQVGGKMIMEYETVLMVDADTRVFPDSIRHMCAEMAKDTNIMGLCGETKI 767
Cdd:pfam03142  162 DSQIILMRFLQKVHFDERMTPLEYELFHQIWNVTGVSPDFYEYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGETKI 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  768 ANKKESWVTAIQVFEYYISHHHSKAFESIFGSVLCLPGCFSMFRIKSPKDkEQTCWVPILANPDIVECYSNNSTDTLHQK 847
Cdd:pfam03142  242 ANKRQSWVTAIQVFEYYISHHLSKAFESVFGGVTCLPGCFSMYRIKAPKG-GDGYWVPILASPDIVEHYSENVVDTLHKK 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  848 NLLLLGEDRYLSSLLLRKFPNRKQVFVPKAACKTVVPSKFLVLLSQRRRWINSTIHNLVDLLRHDNLCGTFCFSMQFVVL 927
Cdd:pfam03142  321 NLLLLGEDRYLTTLMLKTFPKRKTVFVPQAVCKTIAPDTFKVLLSQRRRWINSTVHNLMELVLVRDLCGTFCFSMQFVVF 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  928 LELLGTILLPFAILSTIYVIIYSAL-FAPLPMLTLVLLLVILGLPGVFIVITTTKLVYVVWMLVYLVALPIWNLILPVYA 1006
Cdd:pfam03142  401 IELIGTVVLPAAIAFTVYLIVISILtPDPVPVIPLVLLAAILGLPAILILLTTRKWVYIGWMLVYLLALPIWNFVLPLYA 480
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 2130390345 1007 FWKFDDFSWGETRATKDGKRNDINETAD-TFNHTAVNMMTWKE 1048
Cdd:pfam03142  481 FWHFDDFSWGNTRVVAGEKGKKVHGTDEgEFDPSKIPMKRWEE 523
 
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 ...
531-1048 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: 703.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  531 IIHKNVVkPNNIIHGSSDGF--LNTICFVTCYSEGVRELRSTLDALCTTTYPNTHKLIILVCDGQVTGAHNKKLTSEIAL 608
Cdd:pfam03142    4 IIHKFIA-AQPLGTKRPFGFplKHTICLVTCYSEGEEGLRTTLDSLATTDYPDSHKLLLVICDGMIKGSGNDRSTPDIVL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  609 NMITDFIEDPNEVIPYSYLSIASGAKRFNMAKVYGGYYKYDSD-TVEESQQQQVPIVLVSKCGSFYEIhSSPKPGNRGKR 687
Cdd:pfam03142   83 DMMKDAVIPKEDPEPLSYVAVASGSKRHNMAKVYAGFYEYDGDsHIPEEKQQRVPMIVVVKCGTPSEA-SEKKPGNRGKR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  688 DSQIILMSLLQRAICNERMSELEFQLLKVIWQVGGKMIMEYETVLMVDADTRVFPDSIRHMCAEMAKDTNIMGLCGETKI 767
Cdd:pfam03142  162 DSQIILMRFLQKVHFDERMTPLEYELFHQIWNVTGVSPDFYEYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGETKI 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  768 ANKKESWVTAIQVFEYYISHHHSKAFESIFGSVLCLPGCFSMFRIKSPKDkEQTCWVPILANPDIVECYSNNSTDTLHQK 847
Cdd:pfam03142  242 ANKRQSWVTAIQVFEYYISHHLSKAFESVFGGVTCLPGCFSMYRIKAPKG-GDGYWVPILASPDIVEHYSENVVDTLHKK 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  848 NLLLLGEDRYLSSLLLRKFPNRKQVFVPKAACKTVVPSKFLVLLSQRRRWINSTIHNLVDLLRHDNLCGTFCFSMQFVVL 927
Cdd:pfam03142  321 NLLLLGEDRYLTTLMLKTFPKRKTVFVPQAVCKTIAPDTFKVLLSQRRRWINSTVHNLMELVLVRDLCGTFCFSMQFVVF 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  928 LELLGTILLPFAILSTIYVIIYSAL-FAPLPMLTLVLLLVILGLPGVFIVITTTKLVYVVWMLVYLVALPIWNLILPVYA 1006
Cdd:pfam03142  401 IELIGTVVLPAAIAFTVYLIVISILtPDPVPVIPLVLLAAILGLPAILILLTTRKWVYIGWMLVYLLALPIWNFVLPLYA 480
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 2130390345 1007 FWKFDDFSWGETRATKDGKRNDINETAD-TFNHTAVNMMTWKE 1048
Cdd:pfam03142  481 FWHFDDFSWGNTRVVAGEKGKKVHGTDEgEFDPSKIPMKRWEE 523
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
555-904 1.54e-82

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: 268.02  E-value: 1.54e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  555 CFVTCYSEGVRELRSTLDALCTTTYP--------NTHKLIILVCDGQVTGahnkkltseialnmitdfiedpnevipysy 626
Cdd:cd04190      1 VCVTMYNEDEEELARTLDSILKNDYPfcarggdsWKKIVVCVIFDGAIKK------------------------------ 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  627 lsiasgakrfnmakvyggyykydsdtveesqqqqvpivlvskcgsfyeihsspkpgNRGKRDSQIILMSLLQRaicnerm 706
Cdd:cd04190     51 --------------------------------------------------------NRGKRDSQLWFFNYFCR------- 67
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  707 selefqllkviwqvgGKMIMEYETVLMVDADTRVFPDSIRHMCAEMAKDTNIMGLCGETKIANKKESWVTAIQVFEYYIS 786
Cdd:cd04190     68 ---------------VLFPDDPEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQGPLVMYQVFEYAIS 132
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  787 HHHSKAFESIFGSVLCLPGCFSMFRIKSPKDKEQTcWVPILANPdivecYSNNSTDTLHQKNLLLLGEDRYLSSLLLRKF 866
Cdd:cd04190    133 HWLDKAFESVFGFVTCLPGCFSMYRIEALKGDNGG-KGPLLDYA-----YLTNTVDSLHKKNNLDLGEDRILCTLLLKAG 206
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2130390345  867 PNRKQVFVPKAACKTVVPSKFLVLLSQRRRWINSTIHN 904
Cdd:cd04190    207 PKRKYLYVPGAVAETDVPETFVELLSQRRRWINSTIAN 244
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
852-1019 7.95e-07

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: 52.05  E-value: 7.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  852 LGEDRYLSSLLLRKfpNRKQVFVPKAACKTVVPSKFLVLLSQRRRWINSTIHNLVDLLRHDNLCGTFCFSMQFVVllell 931
Cdd:COG1215    166 LGEDLDLSLRLLRA--GYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLLFLLLLLL----- 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  932 gtillPFAILSTIYVIIYSALFAplpmltlvlllvilglpgVFIVITTTKLVYVVWMLVYLVALPIWNLILpVYAFWKFD 1011
Cdd:COG1215    239 -----PLLLLLLLLALLALLLLL------------------LPALLLALLLALRRRRLLLPLLHLLYGLLL-LLAALRGK 294

                   ....*...
gi 2130390345 1012 DFSWGETR 1019
Cdd:COG1215    295 KVVWKKTP 302
 
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 ...
531-1048 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: 703.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  531 IIHKNVVkPNNIIHGSSDGF--LNTICFVTCYSEGVRELRSTLDALCTTTYPNTHKLIILVCDGQVTGAHNKKLTSEIAL 608
Cdd:pfam03142    4 IIHKFIA-AQPLGTKRPFGFplKHTICLVTCYSEGEEGLRTTLDSLATTDYPDSHKLLLVICDGMIKGSGNDRSTPDIVL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  609 NMITDFIEDPNEVIPYSYLSIASGAKRFNMAKVYGGYYKYDSD-TVEESQQQQVPIVLVSKCGSFYEIhSSPKPGNRGKR 687
Cdd:pfam03142   83 DMMKDAVIPKEDPEPLSYVAVASGSKRHNMAKVYAGFYEYDGDsHIPEEKQQRVPMIVVVKCGTPSEA-SEKKPGNRGKR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  688 DSQIILMSLLQRAICNERMSELEFQLLKVIWQVGGKMIMEYETVLMVDADTRVFPDSIRHMCAEMAKDTNIMGLCGETKI 767
Cdd:pfam03142  162 DSQIILMRFLQKVHFDERMTPLEYELFHQIWNVTGVSPDFYEYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGETKI 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  768 ANKKESWVTAIQVFEYYISHHHSKAFESIFGSVLCLPGCFSMFRIKSPKDkEQTCWVPILANPDIVECYSNNSTDTLHQK 847
Cdd:pfam03142  242 ANKRQSWVTAIQVFEYYISHHLSKAFESVFGGVTCLPGCFSMYRIKAPKG-GDGYWVPILASPDIVEHYSENVVDTLHKK 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  848 NLLLLGEDRYLSSLLLRKFPNRKQVFVPKAACKTVVPSKFLVLLSQRRRWINSTIHNLVDLLRHDNLCGTFCFSMQFVVL 927
Cdd:pfam03142  321 NLLLLGEDRYLTTLMLKTFPKRKTVFVPQAVCKTIAPDTFKVLLSQRRRWINSTVHNLMELVLVRDLCGTFCFSMQFVVF 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  928 LELLGTILLPFAILSTIYVIIYSAL-FAPLPMLTLVLLLVILGLPGVFIVITTTKLVYVVWMLVYLVALPIWNLILPVYA 1006
Cdd:pfam03142  401 IELIGTVVLPAAIAFTVYLIVISILtPDPVPVIPLVLLAAILGLPAILILLTTRKWVYIGWMLVYLLALPIWNFVLPLYA 480
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 2130390345 1007 FWKFDDFSWGETRATKDGKRNDINETAD-TFNHTAVNMMTWKE 1048
Cdd:pfam03142  481 FWHFDDFSWGNTRVVAGEKGKKVHGTDEgEFDPSKIPMKRWEE 523
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
555-904 1.54e-82

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: 268.02  E-value: 1.54e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  555 CFVTCYSEGVRELRSTLDALCTTTYP--------NTHKLIILVCDGQVTGahnkkltseialnmitdfiedpnevipysy 626
Cdd:cd04190      1 VCVTMYNEDEEELARTLDSILKNDYPfcarggdsWKKIVVCVIFDGAIKK------------------------------ 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  627 lsiasgakrfnmakvyggyykydsdtveesqqqqvpivlvskcgsfyeihsspkpgNRGKRDSQIILMSLLQRaicnerm 706
Cdd:cd04190     51 --------------------------------------------------------NRGKRDSQLWFFNYFCR------- 67
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  707 selefqllkviwqvgGKMIMEYETVLMVDADTRVFPDSIRHMCAEMAKDTNIMGLCGETKIANKKESWVTAIQVFEYYIS 786
Cdd:cd04190     68 ---------------VLFPDDPEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQGPLVMYQVFEYAIS 132
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  787 HHHSKAFESIFGSVLCLPGCFSMFRIKSPKDKEQTcWVPILANPdivecYSNNSTDTLHQKNLLLLGEDRYLSSLLLRKF 866
Cdd:cd04190    133 HWLDKAFESVFGFVTCLPGCFSMYRIEALKGDNGG-KGPLLDYA-----YLTNTVDSLHKKNNLDLGEDRILCTLLLKAG 206
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2130390345  867 PNRKQVFVPKAACKTVVPSKFLVLLSQRRRWINSTIHN 904
Cdd:cd04190    207 PKRKYLYVPGAVAETDVPETFVELLSQRRRWINSTIAN 244
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
725-811 5.31e-20

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: 88.44  E-value: 5.31e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  725 IMEYETVLMVDADTRVFPDSIRHMCAEMAKDTNIMGLCGETKIANKKESWVTAIQVFEYYISHHHSKAFESIFGSVLCLP 804
Cdd:cd06423     76 HAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLS 155

                   ....*..
gi 2130390345  805 GCFSMFR 811
Cdd:cd06423    156 GAFGAFR 162
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
731-904 6.32e-08

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: 54.57  E-value: 6.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  731 VLMVDADTRVFPDSIRHMCAEMAkDTNIMGLCGETKIANKKESWVTAIQVFEYYISHHHSKAFESIFGSVLCLPGCFSMF 810
Cdd:cd06434     81 VVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQRILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAY 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  811 RIKspkdkeqtcwvpILANPDivecYSNNSTDTLHQKNLLLLGEDRYLSSLLLRKFpnRKQVFVPKAACKTVVPSKFLVL 890
Cdd:cd06434    160 RTE------------ILKDFL----FLEEFTNETFMGRRLNAGDDRFLTRYVLSHG--YKTVYQYTSEAYTETPENYKKF 221
                          170
                   ....*....|....
gi 2130390345  891 LSQRRRWINSTIHN 904
Cdd:cd06434    222 LKQQLRWSRSNWRS 235
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
730-954 6.58e-07

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: 50.80  E-value: 6.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  730 TVLMVDADTRVFPDSIRHMCAEMAkDTNIMGLCGETKIANKKeSWVTAIQVFEYYISHHHSKAFESIFGSVLCLPGCFSM 809
Cdd:pfam13632    1 WILLLDADTVLPPDCLLGIANEMA-SPEVAIIQGPILPMNVG-NYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  810 FRIkspkdkeqtcwvpilanpDIVEcySNNSTDTLHqknlllLGEDRYLSSLLLRKfpNRKQVFVPKAACKTVVPSKFLV 889
Cdd:pfam13632   79 LRR------------------SALQ--EVGGWDDGS------VSEDFDFGLRLQRA--GYRVRFAPYSAVYEKSPLTFRD 130
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2130390345  890 LLSQRRRWINSTIHNLvDLLRHDNLCGTFCFSMQFVVLLELLgtillpFAILSTIYVIIYSALFA 954
Cdd:pfam13632  131 FLRQRRRWAYGCLLIL-LIRLLGYLGTLLWSGLPLALLLLLL------FSISSLALVLLLLALLA 188
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
852-1019 7.95e-07

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: 52.05  E-value: 7.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  852 LGEDRYLSSLLLRKfpNRKQVFVPKAACKTVVPSKFLVLLSQRRRWINSTIHNLVDLLRHDNLCGTFCFSMQFVVllell 931
Cdd:COG1215    166 LGEDLDLSLRLLRA--GYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLLFLLLLLL----- 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130390345  932 gtillPFAILSTIYVIIYSALFAplpmltlvlllvilglpgVFIVITTTKLVYVVWMLVYLVALPIWNLILpVYAFWKFD 1011
Cdd:COG1215    239 -----PLLLLLLLLALLALLLLL------------------LPALLLALLLALRRRRLLLPLLHLLYGLLL-LLAALRGK 294

                   ....*...
gi 2130390345 1012 DFSWGETR 1019
Cdd:COG1215    295 KVVWKKTP 302
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
728-788 3.82e-03

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


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 39.51  E-value: 3.82e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2130390345  728 YETVLMVDADTRVFPDSIRHMCAEMAKDTNIMGLCGETKiaNKKESWVTAIQVFEYYISHH 788
Cdd:cd06438     82 PDAVVVFDADNLVDPNALEELNARFAAGARVVQAYYNSK--NPDDSWITRLYAFAFLVFNR 140
 
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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