dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Cyphellophora europaea

Lineage

Ascomycota; Eurotiomycetes; ; Cyphellophoraceae; Cyphellophora; Cyphellophora europaea

CAZyme ID

HMPREF1541_00249-t46_1-p1

CAZy Family

AA1

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1882		208525.27	7.1376

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CeuropaeaCBS101466	11153	1220924	59	11094

Gene Location

Enzyme Prediction help

EC	2.4.1.16:11

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT2	1221	1728	1e-246	0.9962049335863378

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
276845	MYSc_Myo17	0.0	30	786	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.
367353	Chitin_synth_2	0.0	1220	1728	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).
214580	MYSc	2.80e-146	27	784	15	670	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	2.57e-82	85	779	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	6.55e-71	1360	1579	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

E-Value	Query Start	Query End	Hit Start
15	1873	8	1875
13	1873	11	1853
13	1873	11	1856
9	1873	5	1851
12	1873	2	1847

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
9.32e-43	85	780	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]
1.42e-42	85	778	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]
1.43e-42	85	780	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]
3.84e-42	85	780	134	726	Rigor myosin X co-complexed with an actin filament [Homo sapiens]
4.50e-42	85	778	80	679	Motor Domain Of Myoe, A Class-i Myosin [Dictyostelium discoideum],1LKX_B Motor Domain Of Myoe, A Class-i Myosin [Dictyostelium discoideum],1LKX_C Motor Domain Of Myoe, A Class-i Myosin [Dictyostelium discoideum],1LKX_D Motor Domain Of Myoe, A Class-i Myosin [Dictyostelium discoideum]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
0.0	39	1873	25	1996	Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
0.0	85	1871	101	1921	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
6.91e-275	885	1769	58	955	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
1.72e-262	883	1739	149	1002	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
2.49e-133	1247	1745	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
1.000074	0.000000

TMHMM Annotations download full data without filtering help

Start	End
900	922
935	954
1206	1228
1599	1621
1631	1653
1660	1682

You are here: Home > Sequence: HMPREF1541_00249-t46_1-p1