CAZyme Information: QRD05891.1

Basic Information

• Species: Parastagonospora nodorum
• Lineage: Ascomycota; Dothideomycetes; ; Phaeosphaeriaceae; Parastagonospora; Parastagonospora nodorum
• CAZyme ID: QRD05891.1
• CAZy Family: GT2
• CAZyme Description: chitin synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1843		205576.85	7.1231

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PnodorumSN15	17580	321614	132	17448

• Gene Location: location=CP069041:841982-847617(+)

Full Sequence      

MAANVLQQPSLPALPTHQQNDTGVTGALASRYHAHLPVALISSHGFVSINTYTDASRGVD
GGKDGSAHQAAEDLAQRAYMRLGQRSEDQVVVFLGDSGSGKTTIRGHMLRSLLSYSATPL
SKKIEHANFVFEAFTTTKSLTTPLASKSGLLLELQYNTSTSNHATLLGAQFLAHRLERSR
IASVPTGERNYHVLYYLLAGTSIAEKKHLHLDLVGDGSAGNRTSIGSNKRWRYLGHPTQL
KVGIDDPKGFQDFKTALRKLEFGKESIAGICEIMATILHIGQLEFETGQSTTPGADDSGG
YSHEGGESLTVVKNKECLAPIAQFLGVAVSDLEQSLRYKSKTLYRERVTVMLDPKGARAN
ADELARALYSLLVTWIMEQMNSRISVLPEEISNTVSLVDFPGFQHSAQTGSSLDQLLNNA
ANENLIAFTQDSFFKRQIQELEAEEVALPGTEFYDNSEAKSGLLKSGNGLLAILDDQMRR
GKTDMQYLDVLRKRFDGKNPSIQPGSSTVVQPGSNFPTPNTSPMFTVRHYCGDVDYSVEG
ILEENAELISGDMINLLKSAQAPFIAQLFGQEALHKMSHPKEKSAIVQATISSKPSRMPS
MARRKADQTGRYGRQVNVFDEDAISDAESNVSGSRKGGSSEKQTGAAGQTVSALRTIDSS
MRKANPYFVFCVKPNERRIANQFDSKCVRAQVQGLGIAEISNRVRKADYSIFLPFAEFLG
LAHTDLAIVGSEKEKVEMILDSKPWRENEVRVGATGVFLSERCWLELANLTDSVPVGRGL
ADSNDNLLTPDANRSYGDARAGLLSPSQGDFYNDKGGNYFGSKDVDARSEAPSGITNGDM
FHGLEQPVIDEKAADKNLEEVEVIPVSGSRKRWMFIVYMMTWMIPDVLIKWIGRIKRPDV
RLAWREKLAINMLIWLSCAFVIFLMIGFPMLICPTQHVYSTAELSSFDGKGKNDAYIAMR
GVVYDLGDFIPAHYPNIIPQKNLEKYAGKDATNLFPVQVSALCTGINGDIHPGVQLNYRT
SNYTASSVNNFISNTDLNAQYHDFRWFTNDSRPDWWFEQQTFLKANYMKGRVGFSPQYLK
TLAGKGDSIAYMNGKVYDLTQYIPGGRDIKPPPPEQGEPDMPKDPNFMDDGVVSIFRVQS
GKDISKYWDGLALDPTKKANMKTCLDNLFYVGELDTRSSAKCLFAKYFLLAISILLVSVI
GFKFLAALQFTRKTDPENIDKFIICTVPAYTEDEDSLRRAIDSAARMKYDDKRKLLVIVC
DGMIIGQGNDKPTPRIVLDILGVPESTDPDPLSFESLGEGQRQHNMGKCYSGLYEVQGHI
VPFLVVVKVGRPSEVSKPGNRGKRDSQIILMRFLNRVHYNLPMSPLELEMHHQIRNIIGV
NPTFYEFLLQIDADTVVAPDAATRFVAAFLHDTRLIAICGETALTNAKSSFITMMQVYEY
YISHNLTKAFESLFGSVTCLPGCFSMYRIRAAETGKPLFVSKEVVEAYQEIRVDTLHTKN
LLHLGEDRFLTTLLMKYHSKYKTKYTMRAHAWTVAPDSWTVFMSQRRRWINSTVHNLIEL
IPLQQLCGFCCFSMRFIVFLDLLSTVVQPVIVVYIGYLIYLLIATPDVVPITAFILLGAI
YGLQMIIFIVRRKWEMIGWMIIYILATPIFAFGLPLYAFWHMDDFSWGNTRLITGEKGQK
IVISDEGKFDPASIPKKRWEEYQAEMWEQHTMRDDRSEVSGYTYATRKPFGGSVAGSEYG
GMPPSRPMSHLDLPRYTSQSRVSLAQSGYGGYEHGIEMAQAANLPTDDVIYNEIRDILST
SDLMTVTKKSVKSELERRFQCDLTLKKMFIGQSVEALLVNGIH

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1198	1705	7.3e-239	0.9962049335863378

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
276845	MYSc_Myo17	0.0	19	764	1	642	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	1197	1705	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	4.76e-143	20	770	18	675	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	3.68e-95	27	760	6	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.
395017	Myosin_head	3.30e-75	74	758	71	672	Myosin head (motor domain).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD05891.1|GT2	0.0	1	1843	1	1843
CAE7027879.1|GT2	0.0	1	1841	1	1841
CBX99340.1|GT2	0.0	108	1830	1	1720
USW53351.1|GT2	0.0	7	1838	5	1843
SMY21508.1|GT2	0.0	1	1838	1	1851

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5I0H_A	6.25e-51	74	761	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]
5I0I_A	1.12e-50	74	761	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]
4A7F_C	6.49e-50	33	759	38	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]
1LKX_A	8.69e-50	33	759	38	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]
5KG8_A	2.67e-49	74	761	134	726	Rigor myosin X co-complexed with an actin filament [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4P9K9|CHS8_USTMA	0.0	24	1838	21	2002	Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
sp|J9VNT4|CHS5_CRYNH	0.0	74	1840	101	1931	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
sp|O13395|CHS6_USTMA	5.88e-269	854	1740	54	947	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VF17|CHS4_CRYNH	1.09e-260	855	1715	148	1001	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
sp|O13353|CHS4_MAGO7	8.01e-130	1224	1744	686	1215	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

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000059	0.000004

TMHMM  Annotations     

Start	End
873	895
908	930
1187	1206
1582	1604
1608	1630
1637	1659