CAZyme Information: OJD19828.1

Basic Information

• Species: Emergomyces pasteurianus
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Emergomyces; Emergomyces pasteurianus
• CAZyme ID: OJD19828.1
• CAZy Family: GT69
• CAZyme Description: Chitin synthase [Source:UniProtKB/TrEMBL;Acc:A0A1J9QVE2]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1866		207083.94	7.5665

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EpasteurianusEp9510	9078	1447872	128	8950

• Gene Location: location=LGRN01000003:32512-38351(+)

Full Sequence      

MALHSFTETGSAPSHAQSSLPSLPAHLQSDTHLTAHLASRFHVSLPTARLSSQGLICLNT
YTSSTRGPDGQREGSAMGEADDLARRAWARLGGRGENQAVIFLGETGSGKTTVRSHLLSS
FLSLSSTPLSAKLSLAAFVFDTLTTTKSVTTPTASKAGLFFELQYDASSTINPTLIGGKL
LDHRLERSRIASVPTGERSFHVLYYLLAGTSAAEKAHLGLDNSVDIRTGGGSGNRSSGTI
SHKRWRYLGHPTQLKVGINDTEGFQQFKTALRKLEFPRSEIAEICQILACILHIGQLEFT
TGQSTTTGPEESGGYSHEGGETVTIVKNKDALAIVAAFLGLSVDDLETSLGYKTKTIHRE
RVTVMLDPKGARENADDLARTLYSLLVAYVIENINQRVCAAEDAVANTISIIDFPGFSQV
SATGSTLDQLLNNAATESLYNYCLRSFFEHRADMLETEEVSVPSTSYFDNSDAVKGLLKQ
GNGLLTILDDQTKRGRSDMQLLESLRKRFANKNPAISVGSATATLPGSNFASKNQAATFT
VRHFAGEVDYPVQGLVEENSDLVSGDLMNLITSSRSAFVRDLFGQEALQTIRHPKEKSAI
MQAQVSSKPLRMPSMARRKMDRPARLTARAAQANNDDDDDIAGSTSSASGSKKRKQGGPA
NGPSQGAAAQFLVSLDNINKSLAAGNVNPYFVFCLKPNDRRIANQFDSKCVRSQVQTFGI
AEISQRLRNADFTVFLPFGEFLGLSDAESIIVGSEQEKCQLVVDERRWPGNEARVGSTGV
FLSERCWADIAKIGERVVPSYSGDGTDDGRDGMLGVGHKAQYGDSKVRLLNSPDTSPSPG
AFIYGDETKQGFYGARDIDGRSDAGASAFNSGDMFKNLETREQMAEKGNEKKMEEVDDVV
VSSSRKRWLAIVYLLTFYIPDFAIKFIGRMKRKDVRTAWREKFAINLLIWFSCAFAVFFI
IGFPQLICPKQYVFSPDELSSRDGKKNDAYIAIRGEVFDLGAFIPSHYPKIVPRKALEKY
AGMDATKLFPVQVSALCDGVDGTIDPSVPLDFTSANRTGSVKVSADHDPNAKYHDFRAFT
DDYRRDWYWNQMRMLRANYKKGYVGYSPQYLKTLVDKDQSIAVLDGYVYDLTNYVIGGRQ
AKAPPGQDPPQGVNVDFMDPLVVDLFQQRPGQDVTELFNRLPLGNRERAMRTCLTNLFQV
GKLDTRSSAQCKFAQYFILAISLLLVTIIAFKFFAALQFGKKNLPENLDKFIICQVPAYT
EDEESLRRAIDSMARMKYDDKRKLLVVICDGMIIGQGNDRPTPRIVLDILGVSETVDPEP
LSFESLGEGMKQHNMGKVYSGLYEVQGHIVPFLVVVKVGKPSEVSRPGNRGKRDSQLLLM
RFLNRVHYNHPMSPLELEIHHQIRNIIGVNPTFYEFIFQVDADTMVAPDSATRMVAAFLQ
DTRIIGLCGETGLNNAKSSIITMIQVYEYYISHNLTKAFESLFGSVTCLPGCFTMYRIRA
ADTGKPLFVSREVVESYSEIRVDTLHMKNLLHLGEDRYLTTLLLKHHSKYKTKFIFNAHA
WTVAPDSWAVFMSQRRRWINSTVHNLIELIPLQQLCGFCCFSMRFVVFVDLLSTVIQPVT
VAYVIYLIVLIAINPSLIPITAFILLGAIYGLQAIIFILRRKWEMVGWMIIYILAMPVFS
LGLPLYSFWHMDDFTWGNTRIVTGEKGRKVVISDEGKFDPSSIPKKKWEDYQAELWDAQT
QADDRSEVSGFSYGTRSYHPAASEYGFSPSRPLSQIELNRFAGSRMSLAPSEMLGHGPEM
EMVDLTGLPSEDSLLAEIRDILRTADLMTVTKKSVKVELERRFNTNLDAKRQYINSATEA
VLSGQL

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1227	1734	6.2e-248	0.9962049335863378

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
276845	MYSc_Myo17	0.0	28	790	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	1226	1734	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	6.15e-143	17	795	11	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.
276950	MYSc	3.50e-73	83	783	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	1.69e-71	1253	1585	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSS67452.1|GT2	0.0	1	1866	1	1866
QSS57527.1|GT2	0.0	1	1866	1	1863
ABV31247.1|GT2	0.0	1	1866	1	1861
AAR88368.1|GT2	0.0	12	1866	4	1857
AAQ05979.1|GT2	0.0	12	1866	4	1857

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5I0H_A	5.18e-46	83	784	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	6.38e-46	83	798	134	740	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	1.61e-45	83	784	134	726	Rigor myosin X co-complexed with an actin filament [Homo sapiens]
4A7F_C	1.87e-39	83	782	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]
1LKX_A	7.87e-39	83	782	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4P9K9|CHS8_USTMA	0.0	37	1863	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	83	1863	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	3.70e-278	896	1752	61	912	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VF17|CHS4_CRYNH	2.12e-273	890	1764	148	1037	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	1.63e-136	1253	1750	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
1.000035	0.000001

TMHMM  Annotations     

Start	End
908	930
943	965
1213	1235
1611	1633
1637	1659
1666	1688