dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Allomyces macrogynus

Lineage

Blastocladiomycota; Blastocladiomycetes; ; Blastocladiaceae; Allomyces; Allomyces macrogynus

CAZyme ID

AMAG_07719-t26_1-p1

CAZy Family

GH26

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1679	GG745340\|CGC3	187511.18	7.2969

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AmacrogynusATCC38327	19333	578462	535	18798

Gene Location

Enzyme Prediction help

EC	2.4.1.16:11

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT2	993	1506	9.3e-236	0.9924098671726755

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	993	1506	4	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	6.43e-128	1	573	78	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.
276950	MYSc	2.30e-89	1	565	68	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.
214580	MYSc	2.82e-89	1	577	86	677	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.
133033	Chitin_synth_C	2.19e-73	1020	1349	3	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
1	1674	97	1891
1	1509	98	1714
1	1678	100	1910
1	1678	100	1910
1	1676	99	1909

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.11e-46	7	338	172	500	Insights into the Importance of Hydrogen Bonding in the Gamma-Phosphate Binding Pocket of Myosin: Structural and Functional Studies of Ser236 [Dictyostelium discoideum],3MYK_X Insights into the Importance of Hydrogen Bonding in the Gamma-Phosphate Binding Pocket of Myosin: Structural and Functional Studies of Ser236 [Dictyostelium discoideum],3MYL_X Insights into the Importance of Hydrogen Bonding in the Gamma-Phosphate Binding Pocket of Myosin: Structural and Functional Studies of Ser236 [Dictyostelium discoideum]
5.92e-46	7	338	172	500	Dictyostelium discoideum Myosin II motor domain S456E with bound MgADP-BeFx [Dictyostelium discoideum]
7.31e-46	7	338	172	500	X-Ray Structures Of The Mgadp, Mgatpgammas, And Mgamppnp Complexes Of The Dictyostelium Discoideum Myosin Motor Domain [Dictyostelium discoideum]
8.06e-46	7	338	171	499	Crystal structure of myosin-2 dictyostelium discoideum motor domain S456Y mutant in complex with adp-orthovanadate [Dictyostelium discoideum]
9.36e-46	7	338	171	499	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]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
0.0	1	1677	95	2005	Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
0.0	1	1674	109	1929	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
2.84e-288	680	1511	57	898	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
8.18e-273	686	1519	155	1004	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
6.03e-145	1020	1506	673	1167	Chitin synthase D OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=chsD PE=1 SV=4

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000060	0.000000

TMHMM Annotations download full data without filtering help

Start	End
734	756
979	1001
1369	1391
1404	1426
1436	1458

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