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CAZyme Information: EHY60832.1

You are here: Home > Sequence: EHY60832.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Exophiala dermatitidis
Lineage Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala dermatitidis
CAZyme ID EHY60832.1
CAZy Family GT71
CAZyme Description chitin synthase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1885 208881.11 7.7149
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_EdermatitidisNIHUT8656 9356 858893 71 9285
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.16:11

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 1215 1722 1.3e-243 0.9962049335863378

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
367353 Chitin_synth_2 0.0 1214 1722 1 527
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).
276845 MYSc_Myo17 0.0 23 781 1 645
class XVII myosin, motor domain. This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
214580 MYSc 1.40e-140 24 782 18 673
Myosin. Large ATPases. ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
276950 MYSc 1.75e-79 78 774 60 633
Myosin motor domain superfamily. Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
133033 Chitin_synth_C 4.36e-68 1354 1573 48 244
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 1885 1 1885
0.0 5 1885 8 1861
0.0 5 1885 10 1866
0.0 5 1885 10 1863
0.0 8 1885 5 1857

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.23e-41 78 775 136 728
Crystal structure of myosin X motor domain in pre-powerstroke state [Homo sapiens],5I0H_B Crystal structure of myosin X motor domain in pre-powerstroke state [Homo sapiens]
1.85e-41 78 775 134 726
Crystal structure of myosin X motor domain with 2IQ motifs in pre-powerstroke state [Homo sapiens],5I0I_B Crystal structure of myosin X motor domain with 2IQ motifs in pre-powerstroke state [Homo sapiens]
1.19e-40 78 775 134 726
Rigor myosin X co-complexed with an actin filament [Homo sapiens]
7.91e-39 78 723 82 627
High-Resolution Cryo-EM Structures of Actin-bound Myosin States Reveal the Mechanism of Myosin Force Sensing [Rattus norvegicus],6C1G_P High-Resolution Cryo-EM Structures of Actin-bound Myosin States Reveal the Mechanism of Myosin Force Sensing [Rattus norvegicus],6C1H_P High-Resolution Cryo-EM Structures of Actin-bound Myosin States Reveal the Mechanism of Myosin Force Sensing [Rattus norvegicus]
7.98e-39 78 773 80 679
Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 3) [Dictyostelium discoideum],4A7F_G Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 3) [Dictyostelium discoideum],4A7F_J Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 3) [Dictyostelium discoideum],4A7H_C Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 2) [Dictyostelium discoideum],4A7H_I Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 2) [Dictyostelium discoideum],4A7H_J Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 2) [Dictyostelium discoideum],4A7L_C Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 1) [Dictyostelium discoideum],4A7L_G Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 1) [Dictyostelium discoideum],4A7L_J Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 1) [Dictyostelium discoideum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 20 1882 8 2003
Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
0.0 78 1882 101 1930
Chitin synthase 5 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=CHS5 PE=2 SV=1
2.13e-278 879 1741 58 912
Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
3.91e-266 877 1775 149 1038
Chitin synthase 4 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=CHS4 PE=2 SV=2
8.86e-133 1241 1739 686 1201
Chitin synthase 4 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=CHS4 PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000055 0.000000

TMHMM  Annotations      download full data without filtering help

Start End
894 916
929 948
1200 1222
1593 1615
1625 1647
1654 1676