dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Batrachochytrium salamandrivorans

Lineage

Chytridiomycota; Chytridiomycetes; ; NA; Batrachochytrium; Batrachochytrium salamandrivorans

CAZyme ID

OON09981.1

CAZy Family

GT59

CAZyme Description

Chitin synthase [Source:UniProtKB/TrEMBL;Acc:A0A1S8W680]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1977		220316.59	6.5268

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

Enzyme Prediction help

EC	2.4.1.16:11

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT2	1312	1816	3.3e-217	0.9867172675521821

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	1312	1816	4	524	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	3.03e-88	133	829	64	646	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	3.14e-75	1336	1668	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	4.05e-65	134	644	55	523	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	2.46e-61	134	829	73	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
6.18e-298	69	1823	21	1697
1.49e-294	134	1816	82	1685
2.08e-290	133	1816	84	1708
4.11e-289	134	1816	91	1670
3.59e-280	133	1816	83	1735

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.20e-34	134	639	153	620	X-Ray Structures Of The Mgadp, Mgatpgammas, And Mgamppnp Complexes Of The Dictyostelium Discoideum Myosin Motor Domain [Dictyostelium discoideum]
2.09e-34	134	639	153	620	CRYSTAL STRUCTURE OF THE APO MOTOR DOMAIN OF DICTYOSTELLIUM MYOSIN II [Dictyostelium discoideum],1FMW_A Crystal Structure Of The Mgatp Complex For The Motor Domain Of Dictyostelium Myosin Ii [Dictyostelium discoideum]
2.72e-34	134	639	152	619	Structural basis for the allosteric interference of myosin function by mutants G680A and G680V of Dictyostelium myosin-2 [Dictyostelium discoideum]
2.72e-34	134	639	152	619	Structural basis for the allosteric interference of myosin function by mutants G680A and G680V of Dictyostelium myosin-2 [Dictyostelium discoideum],2Y8I_X Structural basis for the allosteric interference of myosin function by mutants G680A and G680V of Dictyostelium myosin-2 [Dictyostelium discoideum]
2.77e-34	134	639	153	620	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]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.13e-275	69	1816	17	1746	Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
3.95e-265	133	1816	95	1734	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
2.39e-232	994	1816	62	890	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
1.80e-229	989	1816	152	988	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
1.52e-130	1003	1814	75	951	Chitin synthase 1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=CHS1 PE=2 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000066	0.000000

TMHMM Annotations download full data without filtering help

Start	End
1000	1019
1040	1062
1296	1318
1689	1711
1721	1743
1750	1772

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