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CAZyme Information: OON08435.1

You are here: Home > Sequence: OON08435.1

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 Batrachochytrium salamandrivorans
Lineage Chytridiomycota; Chytridiomycetes; ; NA; Batrachochytrium; Batrachochytrium salamandrivorans
CAZyme ID OON08435.1
CAZy Family GT3
CAZyme Description Chitin synthase [Source:UniProtKB/TrEMBL;Acc:A0A1S8W1Z5]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1800 198676.06 7.6739
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_BsalamandrivoransBS 10186 N/A 51 10135
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 1370 1778 3e-189 0.8026565464895635

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 1368 1772 1 420
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 1.75e-111 61 653 20 555
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.
133033 Chitin_synth_C 8.21e-78 1395 1729 1 244
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.
276950 MYSc 9.93e-73 124 581 55 494
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.
214580 MYSc 1.11e-72 124 623 73 532
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
6.01e-290 56 1772 31 1640
2.31e-288 56 1772 38 1645
2.97e-285 61 1772 39 1581
1.09e-284 25 1772 8 1635
1.09e-284 25 1772 8 1635

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.45e-45 124 581 153 581
Truncated Head Of Myosin From Dictyostelium Discoideum Complexed With Mgadp-Bef3 [Dictyostelium discoideum],1MND_A Truncated Head Of Myosin From Dictyostelium Discoideum Complexed With Mgadp-Alf4 [Dictyostelium discoideum],1MNE_A Truncated Head Of Myosin From Dictyostelium Discoideum Complexed With Mg-Pyrophosphate [Dictyostelium discoideum],1VOM_A Complex Between Dictyostelium Myosin And Mgadp And Vanadate At 1.9a Resolution [Dictyostelium discoideum]
2.08e-45 124 581 153 581
Myosin II Dictyostelium discoideum motor domain S456E bound with MgADP-AlF4 [Dictyostelium discoideum]
2.14e-45 124 581 152 580
Crystal structure of myosin-2 dictyostelium discoideum motor domain S456Y mutant in complex with adp-orthovanadate [Dictyostelium discoideum]
2.54e-45 124 581 153 581
Chain A, MYOSIN S1DC MOTOR DOMAIN [Dictyostelium discoideum],1D0Y_A Chain A, MYOSIN S1DC MOTOR DOMAIN [Dictyostelium discoideum],1D0Z_A Chain A, MYOSIN [Dictyostelium discoideum],1D1A_A Chain A, MYOSIN [Dictyostelium discoideum],1D1B_A Chain A, MYOSIN [Dictyostelium discoideum],1D1C_A Chain A, MYOSIN [Dictyostelium discoideum]
2.57e-45 124 581 153 581
X-Ray Structures Of The Mgadp, Mgatpgammas, And Mgamppnp Complexes Of The Dictyostelium Discoideum Myosin Motor Domain [Dictyostelium discoideum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.27e-281 44 1772 19 1643
Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
1.62e-263 124 1769 96 1628
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
5.27e-203 1048 1772 65 785
Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
1.79e-196 1050 1772 160 884
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
6.34e-114 1391 1772 682 1078
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
1.000051 0.000001

TMHMM  Annotations      download full data without filtering help

Start End
1054 1076
1093 1115
1354 1376
1730 1752
1767 1789