chitin synthase family protein similar to chitin synthase that polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer
Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. ...
318-482
3.91e-99
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: 309.10 E-value: 3.91e-99
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
460-884
7.29e-14
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They catalyze chitin synthesis as follows: UDP-N-acetyl-D-glucosamine + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N) <=> UDP + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N+1).
The actual alignment was detected with superfamily member pfam03142:
Pssm-ID: 367353 [Multi-domain] Cd Length: 527 Bit Score: 75.57 E-value: 7.29e-14
Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. ...
318-482
3.91e-99
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: 309.10 E-value: 3.91e-99
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
314-654
1.11e-80
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: 262.63 E-value: 1.11e-80
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
460-884
7.29e-14
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They catalyze chitin synthesis as follows: UDP-N-acetyl-D-glucosamine + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N) <=> UDP + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N+1).
Pssm-ID: 367353 [Multi-domain] Cd Length: 527 Bit Score: 75.57 E-value: 7.29e-14
Chitin synthase; This region is found commonly in chitin synthases classes I, II and III. ...
318-482
3.91e-99
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: 309.10 E-value: 3.91e-99
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
314-654
1.11e-80
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: 262.63 E-value: 1.11e-80
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
460-884
7.29e-14
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They catalyze chitin synthesis as follows: UDP-N-acetyl-D-glucosamine + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N) <=> UDP + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N+1).
Pssm-ID: 367353 [Multi-domain] Cd Length: 527 Bit Score: 75.57 E-value: 7.29e-14
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
314-549
4.25e-13
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: 68.79 E-value: 4.25e-13
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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