CAZyme Information: EEQ92427.1

Basic Information

• Species: Blastomyces dermatitidis
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Blastomyces; Blastomyces dermatitidis
• CAZyme ID: EEQ92427.1
• CAZy Family: GH55|GH55
• CAZyme Description: chitin synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1865		206837.04	7.4792

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_BdermatitidisER-3	10081	559297	326	9755

• Gene Location: location=EQ999981:897777-903587(+)

Full Sequence      

MALHSLTGTGSIPAHAQSSLPSLPSHLQSDTHLTAHLASRFHVSLPTARLSSQGLICLNT
YTSSTQGPDGQKEGSAMGEADDLARRAWARLGGRGENQAIIFLGETGSGKTTVRSHLLSS
FLALSSTPLSAKLSLAAFVFDTLTTTKSVTTPTASKAGLFFELQYDGSSTVNPTLIGGKL
LDHRLERSRIASVPTGERSFHVLYYLLAGTSPAEKTHLGLDSAIDIRTGGGSGNRSSGTV
SHKRWRYLGHPTQLKVGINDTEGFQQFKNALRKLEFPRSEIAEICQILACILHIGQLEFT
TGQSTTTGPEESGGYSHEGGETVTIVKNKDVLAIIAAFLGLSVDDLEASLGYKTKTIHRE
RVTVMLDPKGARNNADELARTLYSLLVAYVIENINQRVCAAEDAVANTISIIDFPGFSQA
SSTGSALDQLLNNAATESLYNYCLRSFFEYRADMLEIDEVSVPPTSYFDNSDAVKGLLKQ
GNGLLAILDDQTRRGRSDMQLLESLRKRFADKNPAISVGSATATLPGSNFASKNQAANFT
VRHFAGEVDYPVQGLVEENGDLVSGDLMNLITSSRSAFVRDLFGQEALQTIRHPKEKSAI
VQAQVSSKPLRMPSMARRKMDRPVRPTARAAQADNDDVDIAGSTSSASGSKKRKQGALAN
GPSQGAAAQFLVSLDNINKSLAAGSVNPYFVFCLKPNDRRIANQFDSKCVRAQVQTFGIA
EISQRLRNADFTVFLPFSEFLGLSDAESIIVGSEQEKCQLVVDERRWPKNEARVGSTGVF
LSERCWAEVARVGERVVPSYSAGGTDDGRDGLLGVGTKGPYGDSKVRLLNSPDISPSPGA
YIYGDDTKQGFFGGQEIDGRSDAGASAFNSGDMFKNLETREQMAEKGNEKKMEEVDDVVI
SGSRKRWLALVYMLTFYIPDFAIKFFGRMKRKDVRIAWREKFAINLLIWLSCALAVFFII
GFPQLICPKQNVFSPDELSSHDGKNTDAYIAIRGEVFDLGAYIPSHYPKIVPRSALEKYA
GLDATKLFPVQVSALCDGVDGSVDPSVPLDFRSVNRTGSVRVSRDDDPNAKYHDFRAFTE
DSRPDWYWNQMRMLRANYRKGYVGFSPQYLKTLVDQDQSIAVLDGYVYDLSNYVIGGRSP
RAPPGQDPPKDVNVNFMDPLVVDLFQQRPGQDISELFRRLPLGNRERAMRTCLTNLFQVG
KLDTRNSVQCQFAQYFILAISLLLVTIIAFKFFAALQFGKKTLPENLDKFIICQVPAYTE
DEESLRRAIDSMARMKYDDKRKLLVVICDGMIIGQGNDRPTPRIVLDILGVPETVDPEPL
SFESLGEGMKQHNMGKVYSGLYEVQGHIVPFLVVVKVGKPSEVSRPGNRGKRDSQLLLMR
FLNRVHYNHPMSPLELEIHHQIRNIIGVNPTFYEFIFQVDADTMVAPDAATRMVASFMQD
TRIIGLCGETGLNNAKSSIITMIQVYEYYISHNLTKAFESLFGSVTCLPGCFTMYRIRAA
DTGKPLFVSREVVDAYSEIRVDTLHMKNLLHLGEDRYLTTLLLKHHPKYKTKFLFNAHAW
TIAPDSWAVFMSQRRRWINSTVHNLIELIPLQQLCGFCCFSMRFVVFVDLLSTIIQPVTV
AYVIYLIVLIAINPTLIPITAFILLGAIYGLQAIIFILRRKWEMVGWMIIYILAMPVFSL
GLPLYSFWHMDDFTWGNTRIVTGEKGRKVVISDEGKFDPSSIPKKKWEEYQSELWEAQTH
QDDRSEVSGFSYGTRSYHPPASEYGFAPSRPLSQMELNRLAGSRMSVAPSEMLGRGPEME
MVDLAGLPSDDSLLAEIRDILRTADLMTVTKKSVKLELEHRFNVNLDAKRQYINSATEAV
LSGNL

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1226	1733	8.7e-248	0.9962049335863378

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
276845	MYSc_Myo17	0.0	28	789	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	1225	1733	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	1.81e-148	17	794	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	5.45e-73	83	782	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	1.73e-71	1252	1584	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	1865	1	1866
QSS57527.1|GT2	0.0	1	1865	1	1863
ABV31247.1|GT2	0.0	1	1865	1	1861
AAR88368.1|GT2	0.0	13	1865	5	1857
AAQ05979.1|GT2	0.0	13	1865	5	1857

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5I0H_A	6.94e-44	83	783	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	1.09e-43	83	783	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	5.08e-43	83	783	134	726	Rigor myosin X co-complexed with an actin filament [Homo sapiens]
4A7F_C	2.50e-39	83	781	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	1.05e-38	83	781	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	1862	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	1862	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	1.30e-278	892	1736	58	896	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VF17|CHS4_CRYNH	2.51e-275	889	1737	148	995	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	6.91e-135	1252	1735	686	1193	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
1.000045	0.000001

TMHMM  Annotations     

Start	End
907	929
942	964
1212	1234
1610	1632
1636	1658
1665	1687