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Conserved domains on  [gi|281360087|ref|NP_730928|]
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krotzkopf verkehrt, isoform D [Drosophila melanogaster]

Protein Classification

chitin synthase( domain architecture ID 10135803)

chitin synthase catalyzes the formation of chitin polymers in all chitin containing organisms

CAZY:  GT2
Gene Ontology:  GO:0004100|GO:0016757|GO:0006486
SCOP:  3000077

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 ...
583-904 3.89e-91

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: 295.76  E-value: 3.89e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  583 CATMWHETKDEMIEFLKSIMRMDEDQCARrvaqkylrvLDPDYYEFETHIFFDDAFeisdhsdddiqcnrfvklliatmd 662
Cdd:cd04190     2 CVTMYNEDEEELARTLDSILKNDYPFCAR---------GGDSWKKIVVCVIFDGAI------------------------ 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  663 eaaseihqttirlrppkkyptpyggrlvwtlpgktkfithlkdkdRIRHRKRWSQVMYMYYLLGHRLMelpisvdrkdai 742
Cdd:cd04190    49 ---------------------------------------------KKNRGKRDSQLWFFNYFCRVLFP------------ 71
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  743 AENTYLLTLDGDIDFKPNAVTLLVDLMKKNKNLGAACGRIHPVGS--GPMVWYQLFEYAIGHWLQKATEHMIGCVLCSPG 820
Cdd:cd04190    72 DDPEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKkqGPLVMYQVFEYAISHWLDKAFESVFGFVTCLPG 151
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  821 CFSLFRGKALMDDNVMKKY-------TTRSDEARHYVQYDQGEDRWLCTLLLQRGYRVEYS--AASDAYTHCPEGFNEFY 891
Cdd:cd04190   152 CFSMYRIEALKGDNGGKGPlldyaylTNTVDSLHKKNNLDLGEDRILCTLLLKAGPKRKYLyvPGAVAETDVPETFVELL 231
                         330
                  ....*....|...
gi 281360087  892 NQRRRWVPSTIAN 904
Cdd:cd04190   232 SQRRRWINSTIAN 244
 
Name Accession Description Interval E-value
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
583-904 3.89e-91

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: 295.76  E-value: 3.89e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  583 CATMWHETKDEMIEFLKSIMRMDEDQCARrvaqkylrvLDPDYYEFETHIFFDDAFeisdhsdddiqcnrfvklliatmd 662
Cdd:cd04190     2 CVTMYNEDEEELARTLDSILKNDYPFCAR---------GGDSWKKIVVCVIFDGAI------------------------ 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  663 eaaseihqttirlrppkkyptpyggrlvwtlpgktkfithlkdkdRIRHRKRWSQVMYMYYLLGHRLMelpisvdrkdai 742
Cdd:cd04190    49 ---------------------------------------------KKNRGKRDSQLWFFNYFCRVLFP------------ 71
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  743 AENTYLLTLDGDIDFKPNAVTLLVDLMKKNKNLGAACGRIHPVGS--GPMVWYQLFEYAIGHWLQKATEHMIGCVLCSPG 820
Cdd:cd04190    72 DDPEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKkqGPLVMYQVFEYAISHWLDKAFESVFGFVTCLPG 151
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  821 CFSLFRGKALMDDNVMKKY-------TTRSDEARHYVQYDQGEDRWLCTLLLQRGYRVEYS--AASDAYTHCPEGFNEFY 891
Cdd:cd04190   152 CFSMYRIEALKGDNGGKGPlldyaylTNTVDSLHKKNNLDLGEDRILCTLLLKAGPKRKYLyvPGAVAETDVPETFVELL 231
                         330
                  ....*....|...
gi 281360087  892 NQRRRWVPSTIAN 904
Cdd:cd04190   232 SQRRRWINSTIAN 244
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
713-1083 1.06e-22

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: 104.07  E-value: 1.06e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087   713 KRWSQVMYMYYL----LGHRLMELPISVDRKdaIAENT--------YLLTLDGDIDFKPNAVTLLVDLMKKNKNLGAACG 780
Cdd:pfam03142  160 KRDSQIILMRFLqkvhFDERMTPLEYELFHQ--IWNVTgvspdfyeYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCG 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087   781 --RIHPVGSGPMVWYQLFEYAIGHWLQKATEHMIGCVLCSPGCFSLFRGKA-----------LMDDNVMKKYTTRSDEAR 847
Cdd:pfam03142  238 etKIANKRQSWVTAIQVFEYYISHHLSKAFESVFGGVTCLPGCFSMYRIKApkggdgywvpiLASPDIVEHYSENVVDTL 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087   848 HYVQYDQ-GEDRWLCTLLLQR--GYRVEYSAASDAYTHCPEGFNEFYNQRRRWVPSTIANIMDLladakrtIKINDnisL 924
Cdd:pfam03142  318 HKKNLLLlGEDRYLTTLMLKTfpKRKTVFVPQAVCKTIAPDTFKVLLSQRRRWINSTVHNLMEL-------VLVRD---L 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087   925 LYIF-YQMMLMggtilgpgtIFLMLVGAFVaafridnwtsfhyniVPILafmfICFTCKSNIQLFVAQVLSTAYALIMMA 1003
Cdd:pfam03142  388 CGTFcFSMQFV---------VFIELIGTVV---------------LPAA----IAFTVYLIVISILTPDPVPVIPLVLLA 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  1004 VIVGTalqlgedgigsPSAIFLISMVGSFFIAaclhpqefWCitcgLIYLLSIPSMYLLLILYSIINLNVVSWGTREVVA 1083
Cdd:pfam03142  440 AILGL-----------PAILILLTTRKWVYIG--------WM----LVYLLALPIWNFVLPLYAFWHFDDFSWGNTRVVA 496
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
802-985 1.25e-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: 67.46  E-value: 1.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  802 HWLQKATEHM----IGCvlcsPGCFSLFRGKALmddnvmkkyttrsDEARHYVQYDQGEDRWLCTLLLQRGYRVEYSAAS 877
Cdd:COG1215   127 DWLRRLVAAFadpgVGA----SGANLAFRREAL-------------EEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDA 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  878 DAYTHCPEGFNEFYNQRRRWvpstIANIMDLLADAKRTIKINDNISLLYIFYQMMLMGGTILGPGTIFLMLVGAFVAAFR 957
Cdd:COG1215   190 VVYEEAPETLRALFRQRRRW----ARGGLQLLLKHRPLLRPRRLLLFLLLLLLPLLLLLLLLALLALLLLLLPALLLALL 265
                         170       180
                  ....*....|....*....|....*...
gi 281360087  958 IdnWTSFHYNIVPILAFMFICFTCKSNI 985
Cdd:COG1215   266 L--ALRRRRLLLPLLHLLYGLLLLLAAL 291
 
Name Accession Description Interval E-value
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
583-904 3.89e-91

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: 295.76  E-value: 3.89e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  583 CATMWHETKDEMIEFLKSIMRMDEDQCARrvaqkylrvLDPDYYEFETHIFFDDAFeisdhsdddiqcnrfvklliatmd 662
Cdd:cd04190     2 CVTMYNEDEEELARTLDSILKNDYPFCAR---------GGDSWKKIVVCVIFDGAI------------------------ 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  663 eaaseihqttirlrppkkyptpyggrlvwtlpgktkfithlkdkdRIRHRKRWSQVMYMYYLLGHRLMelpisvdrkdai 742
Cdd:cd04190    49 ---------------------------------------------KKNRGKRDSQLWFFNYFCRVLFP------------ 71
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  743 AENTYLLTLDGDIDFKPNAVTLLVDLMKKNKNLGAACGRIHPVGS--GPMVWYQLFEYAIGHWLQKATEHMIGCVLCSPG 820
Cdd:cd04190    72 DDPEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKkqGPLVMYQVFEYAISHWLDKAFESVFGFVTCLPG 151
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  821 CFSLFRGKALMDDNVMKKY-------TTRSDEARHYVQYDQGEDRWLCTLLLQRGYRVEYS--AASDAYTHCPEGFNEFY 891
Cdd:cd04190   152 CFSMYRIEALKGDNGGKGPlldyaylTNTVDSLHKKNNLDLGEDRILCTLLLKAGPKRKYLyvPGAVAETDVPETFVELL 231
                         330
                  ....*....|...
gi 281360087  892 NQRRRWVPSTIAN 904
Cdd:cd04190   232 SQRRRWINSTIAN 244
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
713-1083 1.06e-22

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: 104.07  E-value: 1.06e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087   713 KRWSQVMYMYYL----LGHRLMELPISVDRKdaIAENT--------YLLTLDGDIDFKPNAVTLLVDLMKKNKNLGAACG 780
Cdd:pfam03142  160 KRDSQIILMRFLqkvhFDERMTPLEYELFHQ--IWNVTgvspdfyeYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCG 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087   781 --RIHPVGSGPMVWYQLFEYAIGHWLQKATEHMIGCVLCSPGCFSLFRGKA-----------LMDDNVMKKYTTRSDEAR 847
Cdd:pfam03142  238 etKIANKRQSWVTAIQVFEYYISHHLSKAFESVFGGVTCLPGCFSMYRIKApkggdgywvpiLASPDIVEHYSENVVDTL 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087   848 HYVQYDQ-GEDRWLCTLLLQR--GYRVEYSAASDAYTHCPEGFNEFYNQRRRWVPSTIANIMDLladakrtIKINDnisL 924
Cdd:pfam03142  318 HKKNLLLlGEDRYLTTLMLKTfpKRKTVFVPQAVCKTIAPDTFKVLLSQRRRWINSTVHNLMEL-------VLVRD---L 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087   925 LYIF-YQMMLMggtilgpgtIFLMLVGAFVaafridnwtsfhyniVPILafmfICFTCKSNIQLFVAQVLSTAYALIMMA 1003
Cdd:pfam03142  388 CGTFcFSMQFV---------VFIELIGTVV---------------LPAA----IAFTVYLIVISILTPDPVPVIPLVLLA 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  1004 VIVGTalqlgedgigsPSAIFLISMVGSFFIAaclhpqefWCitcgLIYLLSIPSMYLLLILYSIINLNVVSWGTREVVA 1083
Cdd:pfam03142  440 AILGL-----------PAILILLTTRKWVYIG--------WM----LVYLLALPIWNFVLPLYAFWHFDDFSWGNTRVVA 496
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
802-985 1.25e-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: 67.46  E-value: 1.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  802 HWLQKATEHM----IGCvlcsPGCFSLFRGKALmddnvmkkyttrsDEARHYVQYDQGEDRWLCTLLLQRGYRVEYSAAS 877
Cdd:COG1215   127 DWLRRLVAAFadpgVGA----SGANLAFRREAL-------------EEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDA 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  878 DAYTHCPEGFNEFYNQRRRWvpstIANIMDLLADAKRTIKINDNISLLYIFYQMMLMGGTILGPGTIFLMLVGAFVAAFR 957
Cdd:COG1215   190 VVYEEAPETLRALFRQRRRW----ARGGLQLLLKHRPLLRPRRLLLFLLLLLLPLLLLLLLLALLALLLLLLPALLLALL 265
                         170       180
                  ....*....|....*....|....*...
gi 281360087  958 IdnWTSFHYNIVPILAFMFICFTCKSNI 985
Cdd:COG1215   266 L--ALRRRRLLLPLLHLLYGLLLLLAAL 291
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
741-832 1.65e-09

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: 58.78  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  741 AIAENTYLLTLDGDIDFKPNAVTLLVDLMKKNKNLGAACGRIHPV--GSGPMVWYQLFEYAIGHWLQKATEHMIGCVLCS 818
Cdd:cd06423    75 RHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRngSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVL 154
                          90
                  ....*....|....
gi 281360087  819 PGCFSLFRGKALMD 832
Cdd:cd06423   155 SGAFGAFRREALRE 168
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
747-901 1.03e-07

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: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  747 YLLTLDGDIDFKPNAVTLLVDLMKKNKNLG-AACGRIHPVGSGPMVWYQLFEYAIGHWLQKATEHMIGCVLCSPGCFSLF 825
Cdd:cd06434    80 IVVLLDSDTVWPPNALPEMLKPFEDPKVGGvGTNQRILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTAAY 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087  826 RGKALMD-----DNVMKKYTTRSDEArhyvqydqGEDRWLCTLLLQRGYRVEYSAASDAYTHCPEGFNEFYNQRRRWVPS 900
Cdd:cd06434   160 RTEILKDflfleEFTNETFMGRRLNA--------GDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRS 231

                  .
gi 281360087  901 T 901
Cdd:cd06434   232 N 232
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
747-897 1.49e-06

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: 50.41  E-value: 1.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360087   747 YLLTLDGDIDFKPNAVTLLVDLMKKNKNLGAACGRIHPVGSGPMVWYQLFEYAIGHWLQKATEHMIGCVLCSPGCFSLFR 826
Cdd:pfam13632    1 WILLLDADTVLPPDCLLGIANEMASPEVAIIQGPILPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAFLR 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281360087   827 GKALMDdnvmkkyttrsdearhyVQYDQ----GEDRWLCTLLLQRGYRVEYSAASDAYTHCPEGFNEFYNQRRRW 897
Cdd:pfam13632   81 RSALQE-----------------VGGWDdgsvSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRW 138
 
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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