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Conserved domains on  [gi|1929642041|ref|XP_037143592|]
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uncharacterized protein HG535_0C02140 [Zygotorulaspora mrakii]

Protein Classification

Chitin_synth_1N and Chitin_synth_C domain-containing protein( domain architecture ID 13750338)

Chitin_synth_1N and Chitin_synth_C domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
291-609 4.51e-96

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: 302.69  E-value: 4.51e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 291 ICVTMYNEDKFAVARTIDSIMRNISHLCGRmkssvwGPDGWKKISVILISDGRSKVNQgaldylaalgvyqedmakesvn 370
Cdd:cd04190     1 VCVTMYNEDEEELARTLDSILKNDYPFCAR------GGDSWKKIVVCVIFDGAIKKNR---------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 371 gdsvkahifelttqvsinanldyvsndivpvqmifclkeenkKKINSHRWLFNAFCPVL---QPHIVTLIDIGTRLNDTA 447
Cdd:cd04190    53 ------------------------------------------GKRDSQLWFFNYFCRVLfpdDPEFILLVDADTKFDPDS 90
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 448 VYHLWKVFDMDSNVAGAAGQIKTMKgkwglKLLNPLVASQNFEYKISNILDKPLESSFGYISVLPGALSAYRYRALKNHE 527
Cdd:cd04190    91 IVQLYKAMDKDPEIGGVCGEIHPMG-----KKQGPLVMYQVFEYAISHWLDKAFESVFGFVTCLPGCFSMYRIEALKGDN 165
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 528 DGTGPLNSYflGETQEGRDHDVFTANMYLAEDRILCWELVAKRDAKWVLkYVKEATGETDVPEDIPEFISQRRRWLNGAM 607
Cdd:cd04190   166 GGKGPLLDY--AYLTNTVDSLHKKNNLDLGEDRILCTLLLKAGPKRKYL-YVPGAVAETDVPETFVELLSQRRRWINSTI 242

                  ..
gi 1929642041 608 FA 609
Cdd:cd04190   243 AN 244
Chitin_synth_1N pfam08407
Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).
234-294 8.74e-26

Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).


:

Pssm-ID: 462467  Cd Length: 70  Bit Score: 101.01  E-value: 8.74e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1929642041 234 LKLDNPIPRGLLDTLPRR-DSPEFTEMRYTACTVDADQFSQEGYTLRFAEMNRECQIAICVT 294
Cdd:pfam08407   9 LVLDCPVPSRLLNALPRRkGSREFTHMRYTAVTCDPDDFTKNGYTLRQALYGRETELFIVIT 70
Chitin_synth_2 super family cl37687
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
433-831 2.92e-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).


The actual alignment was detected with superfamily member pfam03142:

Pssm-ID: 367353 [Multi-domain]  Cd Length: 527  Bit Score: 79.80  E-value: 2.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 433 IVTLIDIGTRLNDTAVYHLWKVFDMDSNVAGAAGQ--IKTMKGKWglkllnpLVASQNFEYKISNILDKPLESSFGYISV 510
Cdd:pfam03142 204 YVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGEtkIANKRQSW-------VTAIQVFEYYISHHLSKAFESVFGGVTC 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 511 LPGALSAYRYRALKNHEDGTGPL--NSYFLGETQEGRDHDVFTAN-MYLAEDRILCwELVAKRDAKWVLKYVKEATGETD 587
Cdd:pfam03142 277 LPGCFSMYRIKAPKGGDGYWVPIlaSPDIVEHYSENVVDTLHKKNlLLLGEDRYLT-TLMLKTFPKRKTVFVPQAVCKTI 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 588 VPEDIPEFISQRRRWLNgamfaalyaqlhfyhiwKTKHSvtrkiffhieffyqfvqmLFSWFAISNFVLTFYYlagSMng 667
Cdd:pfam03142 356 APDTFKVLLSQRRRWIN-----------------STVHN------------------LMELVLVRDLCGTFCF---SM-- 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 668 vikhgnavfiffKYLIFCDLaslfiismgnrpqgakhlfIASMII-LTICAAYALIcgfVFSIralqskseSSSVFTNII 746
Cdd:pfam03142 396 ------------QFVVFIEL-------------------IGTVVLpAAIAFTVYLI---VISI--------LTPDPVPVI 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 747 -ISLLSTygVYTLTSILYL---DPWHMLTSSVQYFFSLPAFTCTLQIFSFCNTHDVSWGTKGSTQSSKPLSKAIVVQGP- 821
Cdd:pfam03142 434 pLVLLAA--ILGLPAILILlttRKWVYIGWMLVYLLALPIWNFVLPLYAFWHFDDFSWGNTRVVAGEKGKKVHGTDEGEf 511
                         410
                  ....*....|
gi 1929642041 822 DGKQIVETDW 831
Cdd:pfam03142 512 DPSKIPMKRW 521
 
Name Accession Description Interval E-value
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
291-609 4.51e-96

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: 302.69  E-value: 4.51e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 291 ICVTMYNEDKFAVARTIDSIMRNISHLCGRmkssvwGPDGWKKISVILISDGRSKVNQgaldylaalgvyqedmakesvn 370
Cdd:cd04190     1 VCVTMYNEDEEELARTLDSILKNDYPFCAR------GGDSWKKIVVCVIFDGAIKKNR---------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 371 gdsvkahifelttqvsinanldyvsndivpvqmifclkeenkKKINSHRWLFNAFCPVL---QPHIVTLIDIGTRLNDTA 447
Cdd:cd04190    53 ------------------------------------------GKRDSQLWFFNYFCRVLfpdDPEFILLVDADTKFDPDS 90
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 448 VYHLWKVFDMDSNVAGAAGQIKTMKgkwglKLLNPLVASQNFEYKISNILDKPLESSFGYISVLPGALSAYRYRALKNHE 527
Cdd:cd04190    91 IVQLYKAMDKDPEIGGVCGEIHPMG-----KKQGPLVMYQVFEYAISHWLDKAFESVFGFVTCLPGCFSMYRIEALKGDN 165
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 528 DGTGPLNSYflGETQEGRDHDVFTANMYLAEDRILCWELVAKRDAKWVLkYVKEATGETDVPEDIPEFISQRRRWLNGAM 607
Cdd:cd04190   166 GGKGPLLDY--AYLTNTVDSLHKKNNLDLGEDRILCTLLLKAGPKRKYL-YVPGAVAETDVPETFVELLSQRRRWINSTI 242

                  ..
gi 1929642041 608 FA 609
Cdd:cd04190   243 AN 244
Chitin_synth_1 pfam01644
Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. ...
295-455 4.18e-93

Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. Chitin a linear homopolymer of GlcNAc residues, it is an important component of the cell wall of fungi and is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases.


Pssm-ID: 426363  Cd Length: 163  Bit Score: 291.38  E-value: 4.18e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 295 MYNEDKFAVARTIDSIMRNISHLCGRMKSSVWGPDGWKKISVILISDGRSKVNQGALDYLAALGVYQEDMAKESVNGDSV 374
Cdd:pfam01644   1 MYNEDEILLARTLHGVMKNIAHLCSRKRSKTWGPDGWKKVVVCIVSDGRNKINPRTLDLLAALGVYQEGIAKNDVNGKPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 375 KAHIFELTTQVSINA--NLDYVSNDIVPVQMIFCLKEENKKKINSHRWLFNAFCPVLQPHIVTLIDIGTRLNDTAVYHLW 452
Cdd:pfam01644  81 TAHLFEYTTQLSVDEdlKFKGNEKGIVPVQIIFCLKEKNAKKINSHRWFFNAFGPLLQPNVCVLLDVGTKPGPTSIYHLW 160

                  ...
gi 1929642041 453 KVF 455
Cdd:pfam01644 161 KAF 163
Chitin_synth_1N pfam08407
Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).
234-294 8.74e-26

Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).


Pssm-ID: 462467  Cd Length: 70  Bit Score: 101.01  E-value: 8.74e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1929642041 234 LKLDNPIPRGLLDTLPRR-DSPEFTEMRYTACTVDADQFSQEGYTLRFAEMNRECQIAICVT 294
Cdd:pfam08407   9 LVLDCPVPSRLLNALPRRkGSREFTHMRYTAVTCDPDDFTKNGYTLRQALYGRETELFIVIT 70
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
433-831 2.92e-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: 79.80  E-value: 2.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 433 IVTLIDIGTRLNDTAVYHLWKVFDMDSNVAGAAGQ--IKTMKGKWglkllnpLVASQNFEYKISNILDKPLESSFGYISV 510
Cdd:pfam03142 204 YVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGEtkIANKRQSW-------VTAIQVFEYYISHHLSKAFESVFGGVTC 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 511 LPGALSAYRYRALKNHEDGTGPL--NSYFLGETQEGRDHDVFTAN-MYLAEDRILCwELVAKRDAKWVLKYVKEATGETD 587
Cdd:pfam03142 277 LPGCFSMYRIKAPKGGDGYWVPIlaSPDIVEHYSENVVDTLHKKNlLLLGEDRYLT-TLMLKTFPKRKTVFVPQAVCKTI 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 588 VPEDIPEFISQRRRWLNgamfaalyaqlhfyhiwKTKHSvtrkiffhieffyqfvqmLFSWFAISNFVLTFYYlagSMng 667
Cdd:pfam03142 356 APDTFKVLLSQRRRWIN-----------------STVHN------------------LMELVLVRDLCGTFCF---SM-- 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 668 vikhgnavfiffKYLIFCDLaslfiismgnrpqgakhlfIASMII-LTICAAYALIcgfVFSIralqskseSSSVFTNII 746
Cdd:pfam03142 396 ------------QFVVFIEL-------------------IGTVVLpAAIAFTVYLI---VISI--------LTPDPVPVI 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 747 -ISLLSTygVYTLTSILYL---DPWHMLTSSVQYFFSLPAFTCTLQIFSFCNTHDVSWGTKGSTQSSKPLSKAIVVQGP- 821
Cdd:pfam03142 434 pLVLLAA--ILGLPAILILlttRKWVYIGWMLVYLLALPIWNFVLPLYAFWHFDDFSWGNTRVVAGEKGKKVHGTDEGEf 511
                         410
                  ....*....|
gi 1929642041 822 DGKQIVETDW 831
Cdd:pfam03142 512 DPSKIPMKRW 521
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
556-701 1.28e-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: 54.36  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 556 LAEDRILCWELVAkrdAKWVLKYVKEATGETDVPEDIPEFISQRRRWLNGAMfaalyaQLHFYHIWktkhsVTRKIFFHI 635
Cdd:COG1215   166 LGEDLDLSLRLLR---AGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGL------QLLLKHRP-----LLRPRRLLL 231
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1929642041 636 EFFYQFVQMLFSWFAISNFVLTFYYLAGSMNGVIKHGNAVFIFFKYLIFCDLASLFIISMGNRPQG 701
Cdd:COG1215   232 FLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAALRGKKVV 297
 
Name Accession Description Interval E-value
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
291-609 4.51e-96

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: 302.69  E-value: 4.51e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 291 ICVTMYNEDKFAVARTIDSIMRNISHLCGRmkssvwGPDGWKKISVILISDGRSKVNQgaldylaalgvyqedmakesvn 370
Cdd:cd04190     1 VCVTMYNEDEEELARTLDSILKNDYPFCAR------GGDSWKKIVVCVIFDGAIKKNR---------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 371 gdsvkahifelttqvsinanldyvsndivpvqmifclkeenkKKINSHRWLFNAFCPVL---QPHIVTLIDIGTRLNDTA 447
Cdd:cd04190    53 ------------------------------------------GKRDSQLWFFNYFCRVLfpdDPEFILLVDADTKFDPDS 90
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 448 VYHLWKVFDMDSNVAGAAGQIKTMKgkwglKLLNPLVASQNFEYKISNILDKPLESSFGYISVLPGALSAYRYRALKNHE 527
Cdd:cd04190    91 IVQLYKAMDKDPEIGGVCGEIHPMG-----KKQGPLVMYQVFEYAISHWLDKAFESVFGFVTCLPGCFSMYRIEALKGDN 165
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 528 DGTGPLNSYflGETQEGRDHDVFTANMYLAEDRILCWELVAKRDAKWVLkYVKEATGETDVPEDIPEFISQRRRWLNGAM 607
Cdd:cd04190   166 GGKGPLLDY--AYLTNTVDSLHKKNNLDLGEDRILCTLLLKAGPKRKYL-YVPGAVAETDVPETFVELLSQRRRWINSTI 242

                  ..
gi 1929642041 608 FA 609
Cdd:cd04190   243 AN 244
Chitin_synth_1 pfam01644
Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. ...
295-455 4.18e-93

Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. Chitin a linear homopolymer of GlcNAc residues, it is an important component of the cell wall of fungi and is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases.


Pssm-ID: 426363  Cd Length: 163  Bit Score: 291.38  E-value: 4.18e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 295 MYNEDKFAVARTIDSIMRNISHLCGRMKSSVWGPDGWKKISVILISDGRSKVNQGALDYLAALGVYQEDMAKESVNGDSV 374
Cdd:pfam01644   1 MYNEDEILLARTLHGVMKNIAHLCSRKRSKTWGPDGWKKVVVCIVSDGRNKINPRTLDLLAALGVYQEGIAKNDVNGKPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 375 KAHIFELTTQVSINA--NLDYVSNDIVPVQMIFCLKEENKKKINSHRWLFNAFCPVLQPHIVTLIDIGTRLNDTAVYHLW 452
Cdd:pfam01644  81 TAHLFEYTTQLSVDEdlKFKGNEKGIVPVQIIFCLKEKNAKKINSHRWFFNAFGPLLQPNVCVLLDVGTKPGPTSIYHLW 160

                  ...
gi 1929642041 453 KVF 455
Cdd:pfam01644 161 KAF 163
Chitin_synth_1N pfam08407
Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).
234-294 8.74e-26

Chitin synthase N-terminal; This is the N-terminal domain of Chitin synthase (pfam01644).


Pssm-ID: 462467  Cd Length: 70  Bit Score: 101.01  E-value: 8.74e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1929642041 234 LKLDNPIPRGLLDTLPRR-DSPEFTEMRYTACTVDADQFSQEGYTLRFAEMNRECQIAICVT 294
Cdd:pfam08407   9 LVLDCPVPSRLLNALPRRkGSREFTHMRYTAVTCDPDDFTKNGYTLRQALYGRETELFIVIT 70
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
293-540 4.19e-17

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: 79.96  E-value: 4.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 293 VTMYNEDKfAVARTIDSIMRNIshlcgrmkssvwgpdgWKKISVILISDGRSkvnQGALDYLAALGvyqedmakesvngd 372
Cdd:cd06423     3 VPAYNEEA-VIERTIESLLALD----------------YPKLEVIVVDDGST---DDTLEILEELA-------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 373 svkahifelttqvsinanldyvsnDIVPVQMIFCLKEENKKKINSHrwlfNAFCPVLQPHIVTLIDIGTRLNDTAVYHLW 452
Cdd:cd06423    49 ------------------------ALYIRRVLVVRDKENGGKAGAL----NAGLRHAKGDIVVVLDADTILEPDALKRLV 100
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 453 KVFDMDSNVAGAAGQIKTMKGKwglklLNPLVASQNFEYKISNILDKPLESSFGYISVLPGALSAYRYRALKNHedgtGP 532
Cdd:cd06423   101 VPFFADPKVGAVQGRVRVRNGS-----ENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAFGAFRREALREV----GG 171

                  ....*...
gi 1929642041 533 LNSYFLGE 540
Cdd:cd06423   172 WDEDTLTE 179
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
433-831 2.92e-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: 79.80  E-value: 2.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 433 IVTLIDIGTRLNDTAVYHLWKVFDMDSNVAGAAGQ--IKTMKGKWglkllnpLVASQNFEYKISNILDKPLESSFGYISV 510
Cdd:pfam03142 204 YVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGEtkIANKRQSW-------VTAIQVFEYYISHHLSKAFESVFGGVTC 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 511 LPGALSAYRYRALKNHEDGTGPL--NSYFLGETQEGRDHDVFTAN-MYLAEDRILCwELVAKRDAKWVLKYVKEATGETD 587
Cdd:pfam03142 277 LPGCFSMYRIKAPKGGDGYWVPIlaSPDIVEHYSENVVDTLHKKNlLLLGEDRYLT-TLMLKTFPKRKTVFVPQAVCKTI 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 588 VPEDIPEFISQRRRWLNgamfaalyaqlhfyhiwKTKHSvtrkiffhieffyqfvqmLFSWFAISNFVLTFYYlagSMng 667
Cdd:pfam03142 356 APDTFKVLLSQRRRWIN-----------------STVHN------------------LMELVLVRDLCGTFCF---SM-- 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 668 vikhgnavfiffKYLIFCDLaslfiismgnrpqgakhlfIASMII-LTICAAYALIcgfVFSIralqskseSSSVFTNII 746
Cdd:pfam03142 396 ------------QFVVFIEL-------------------IGTVVLpAAIAFTVYLI---VISI--------LTPDPVPVI 433
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 747 -ISLLSTygVYTLTSILYL---DPWHMLTSSVQYFFSLPAFTCTLQIFSFCNTHDVSWGTKGSTQSSKPLSKAIVVQGP- 821
Cdd:pfam03142 434 pLVLLAA--ILGLPAILILlttRKWVYIGWMLVYLLALPIWNFVLPLYAFWHFDDFSWGNTRVVAGEKGKKVHGTDEGEf 511
                         410
                  ....*....|
gi 1929642041 822 DGKQIVETDW 831
Cdd:pfam03142 512 DPSKIPMKRW 521
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
556-701 1.28e-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: 54.36  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 556 LAEDRILCWELVAkrdAKWVLKYVKEATGETDVPEDIPEFISQRRRWLNGAMfaalyaQLHFYHIWktkhsVTRKIFFHI 635
Cdd:COG1215   166 LGEDLDLSLRLLR---AGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGL------QLLLKHRP-----LLRPRRLLL 231
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1929642041 636 EFFYQFVQMLFSWFAISNFVLTFYYLAGSMNGVIKHGNAVFIFFKYLIFCDLASLFIISMGNRPQG 701
Cdd:COG1215   232 FLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAALRGKKVV 297
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
433-602 6.13e-06

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: 48.40  E-value: 6.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 433 IVTLIDIGTRLNDTAVYHLWKVFDmDSNVAGAAGQIKTMK--GKWGLKLLNPLVASQNFEYKISNildkpleSSFGYISV 510
Cdd:cd06434    80 IVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQRILRprDSKWSFLAAEYLERRNEEIRAAM-------SYDGGVPC 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929642041 511 LPGALSAYRYRALKNHEdgtgpLNSYFLGETQEGRdhdvftaNMYLAEDRILCWELVAKrdaKWVLKYVKEATGETDVPE 590
Cdd:cd06434   152 LSGRTAAYRTEILKDFL-----FLEEFTNETFMGR-------RLNAGDDRFLTRYVLSH---GYKTVYQYTSEAYTETPE 216
                         170
                  ....*....|..
gi 1929642041 591 DIPEFISQRRRW 602
Cdd:cd06434   217 NYKKFLKQQLRW 228
 
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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