CAZyme Information: KID61902.1

Basic Information

• Species: Metarhizium anisopliae
• Lineage: Ascomycota; Sordariomycetes; ; Clavicipitaceae; Metarhizium; Metarhizium anisopliae
• CAZyme ID: KID61902.1
• CAZy Family: AA7
• CAZyme Description: class V chitin synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1858	AZNF01000013|CGC5	205610.25	7.1654

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ManisopliaeARSEF549	10891	1276135	0	10891

• Gene Location: location=AZNF01000013:296710-302431(-)

Full Sequence      

MASTLPPLGAGNGGAHTQHSLPSLPAHLQSDTHITGHLASRFHVSHPTAKLSSHALVCLN
TYTSSSKGPDGGKPGSAMAGAEDMADRAWIRLGHRSENQAVVFLGESGSGKSTIRSHLLT
ALLDKSSTPLSNKLSLAAYVFDSLTTTKTATTPTASKSGLFYELQYDTSATTNPILIGGK
LLDHRLERSRIADVPTGERNFHVLYYLLAGTSQAEKTHLGLDDGASGSKRWKYLGHPTQL
KVGINDSEGFQLFKTALKKLEFPRTDIAEICQILAAILHIGQLEFESTNNTSATGDDSGG
FSHEGGQTSTTVRNKDVLGIIAAFLGVSAADLQSTLGYKTKMIQKERVTVMLDPAGARAH
ANELARTLYSLLVAWILESVNQRICAPEEDIANTISIVDFPGFAQQTATGSTLDQLLNNA
ATEAIYNFTLHNFFDRKAEMLESEEVSVAPTSYFDNSDAVKGLLKSGNGLLSILDDQTRR
NKTDIQLLESLRKRFEGKNPAIEVGSATAKLPGSNFYTENAAASFTVRHFAGEVEYPVKG
LIEENGEVVSVDLLNMFNSTKSEFVGRLFGQDVLQTVNHPIEKSTVMQATISSKPMRAPS
VMSRKGGRGRGIASQRRQQESNLFDSGNTHAESRSPKGGNKGGIDQGASGQFLSSLDNVQ
KAVTDPGTNAYFVFCLKPNDRRIANQFDSKCVRTQVQTFGIAEISQRLRSADFSLFLPFG
EFLGMADAETILVGSERERAEMVIEEKRWPSNEIQIGSTGVFLSERCWMEVARLVDVSAA
QGRFALPSSDGYGNDGATPGERDAFGASKEQLLSGGNTPLMYGEKGRPGYFGSDDARSEA
GASAIGGGDMFKNFDTREQMAERGNEKNLEEIEEFKDSPSRKRWVFTVYFLTWFIPDFLI
RWMGRMPRKDVRMAWREKLAINMLIWFMCLVAAFFIVVFPMLICPKQNVFSAAELSSHDG
KDGNSAYVSVRGYVIDLGSFADRHYPSFVSRKTMLNYAGMDVSSLFPVQVSALCQGTDGS
VDQAVTLDYKNINMTGSPALINSQDLNAQYHDFRYFTNDTRPDWYLEQLIMLKGNYGKGT
IGYSPEYLAKLGAKRQVIASIGSRVYDLTAYTVGGRRLRVKPGESLPSDPKLADFMDQKV
VALFQSQAGGDITKFWNSLALAPDVKARMQTCLDHLFYVGDVDTRNSTRCKFAEYLVLAV
SILLVSVIAFKFFAALQFGGKNVPENLDKFVMCQIPAYTEDEDSLRRAIDSAARMRYDDK
RKLLVIVCDGMIIGQGNDRPTPRIVLDILGVSETVDPEPLSFESLGEGLKQHNMGKVYSG
LYEVQGHIVPFLVIVKVGKPSEVARPGNRGKRDSQMILMRFLNRVHYNLAMSPLELEMYH
QIRNIIGVNPTFYEFMLQIDADTVVAPDSATRMVSAFLDDTRLIAVCGETALTNAKSSFI
TMIQVYEYYISHNLSKAFESLFGSVTCLPGCFSMYRIRAAETGKPLFVSREVVDSYATIR
VDTLHMKNLLHLGEDRYLTTLLLKYHSKYKTKYLFSAHAWTIAPDSWKVFLSQRRRWINS
TVHNLMELIPMAQLCGFCCFSMRFVVFIDLLSTVVQPVTIAYIAYLIVLVATKTTVVPIT
AFILLGAIYGLQAIIFILRRKWEMVGWMILYVMAVPVFSFGLPLYAFWHMDDFNWGTTRV
VAGEKGKKVVISDEGKFDPSSIPRKKWEEYQAELWETQTSRDDSRSEISGISYGTKAQAV
VSEYGFPSRPDSTTGFAAHALPYDSRNNSRMSLAHSDIGHHRMSQFGGSQFFNPDDMVGL
PSDDALLAEIRDILKTADLMTVTKKGIKQELERRFDVPLDAKRAYINSATEALLSGQL

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1206	1713	1.6e-248	0.9962049335863378

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
276845	MYSc_Myo17	0.0	29	768	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	1205	1713	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	1.08e-138	21	774	14	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	7.14e-81	84	764	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	1.91e-69	1344	1564	47	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLI64230.1|GT2	0.0	1	1858	1	1858
ABF20219.1|GT2	0.0	1	1858	1	1860
QPH04447.1|GT2	0.0	1	1858	1	1860
QUC16698.1|GT2	0.0	1	1858	1	1863
ANH56571.1|GT2	0.0	2	1851	3	1860

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5I0H_A	2.18e-43	84	765	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	3.39e-43	84	765	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]
5KG8_A	8.97e-43	84	765	134	726	Rigor myosin X co-complexed with an actin filament [Homo sapiens]
6C1D_P	5.94e-40	84	763	82	682	High-Resolution Cryo-EM Structures of Actin-bound Myosin States Reveal the Mechanism of Myosin Force Sensing [Rattus norvegicus],6C1G_P High-Resolution Cryo-EM Structures of Actin-bound Myosin States Reveal the Mechanism of Myosin Force Sensing [Rattus norvegicus],6C1H_P High-Resolution Cryo-EM Structures of Actin-bound Myosin States Reveal the Mechanism of Myosin Force Sensing [Rattus norvegicus]
4L79_A	6.74e-40	84	763	87	687	Crystal Structure of nucleotide-free Myosin 1b residues 1-728 with bound Calmodulin [Rattus norvegicus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4P9K9|CHS8_USTMA	0.0	38	1855	25	2003	Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
sp|J9VNT4|CHS5_CRYNH	0.0	84	1855	101	1930	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	9.33e-281	869	1790	58	981	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VF17|CHS4_CRYNH	1.67e-264	866	1724	148	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
sp|O13353|CHS4_MAGO7	9.62e-133	1232	1730	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

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000051	0.000001

TMHMM  Annotations     

Start	End
884	903
924	943
1192	1214
1584	1606
1616	1638
1645	1667