CAZyme Information: CNBF3100-t26_1-p1

Basic Information

• Species: Cryptococcus neoformans
• Lineage: Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus neoformans
• CAZyme ID: CNBF3100-t26_1-p1
• CAZy Family: GH31
• CAZyme Description: putative chitin synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1895	CM000045|CGC2	214416.52	6.8531

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CneoformansB-3501A	6608	283643	108	6500

• Gene Location: location=CM000045:928351-934767(-)

Full Sequence      

MAQQPPPSRFQGVTDLSPYSYLPIDGEESLLRYVEEYYQCNNEEGGSRNEQGWWKKKLEE
PHVFQLALGAYYNMRRTGQDQVIIASGPTGSGKSELKRLAIEAITQVSLANPGKKGSKIG
LQVSSAEFILKCFGNAHTLSNDEASRFGTYTELQFNERGRLEGLKTIVYYFERSRVSQVP
INGERNFHAFYYLVSGAPEEERNFLKLGDVSDYRYLNCRVRRVGVDDRHRYSQLRQAFKM
IGISSRLIAQIFQLLASILHIGNLRFSPSDGIQEGASVINMDTLDTVAEFLGVHSESLAE
IFSLKTILVRKEVCTTFLGPEQAEQVRDELARTLYSLLFSWLNEHINTRLCKDSFGSFIA
LVDLPGIQRNSGSMGSLNSVDQFCLNFAAEKMHNWVLHRIHETTRQEAEAERLLISRVPY
FDNSECLGMLSNPRGGLISVIDDLSQKKRSESNLLESLGKRFHNHPSMSISPQGNRSSAS
FTINHYDGPVTYSTSNFLERNANETSTDIIQLLRGDTTSRSQVSTTEGHGSSNPFIKGLF
GMKNIAMQTHPRSDSTIVAAQQSVRPVRAPSTRRKKMMSLVPVSEEGGEEASDFQVGGGN
DESSPKELHCIAGQHWAAVDSLLKSFDQTQTWYIFALRPNDSQLPFQFDLRSMKQQVRSF
GLVEMAQQLQTSWEVRLPHKEACERYNEELVYRGIPEGTGDVERLRDLKRLMSLNDADMG
IGLQRVFLSNNLFHFLEDRLRAKEPGEQHAYEDLGHRKLQTDPFSPHRYQPATFDSQEHV
YRDPSIRPVDSSSNLPLMEHARPIVNNSLEIDDHESSPVPYISYGGRSITDIEGYASSRD
LLASSIHKSEKDPLDTEPQAGETTEVYRESIARRRWVWLCSILTWWIPGFVLSKIAGMKR
QDIRQAWREKLAINMIIWFICGCAIFVIAILGPIICPTQHVYSASELASHSYTLDPNNAF
VAIRGEVFDLSQFAPTHLTAVSVVPTKSIMQYGGLDASELFPVQVSALCGGVSGSISQYV
TLDSTNTTDVYSQYHDFRAYTNDSRPDWYAEMMIMMRHRFRVGFMGYTKKDLKTMAAQGK
AVAIYDNLVYDMSNYIRQNGGGLRAPDGVNLTAQDQADRQFMSDQVVSLFKYNSGKDITT
LLDNLGSTIGTDVVDRQKTCLRNLFILGKLDTRDSAQCQFSTYILLALSCVMVAVIGFKF
LSALHFGSVRAPESHDKFVICQVPCYTEGEESLRRTIDSLCKLRYDDKRKLILVICDGNI
KGFGNDKPTPAIVLDILGVDVNNDPEPLSFQSLGEGAKQHNMGKVYAGLYECAGHVVPYL
VIAKVGKPNERQKPGNRGKRDSQMLVMHFLNKVHFSAPMNPLELEMYHQIKNVIGVNPSF
YEYLFMVDADTTVDEMSLNRLVSAMRHDKKIIGVCGETSIANAKQSIVTMSQVYEYFISH
HLSKAFESLFGSITCLPGCFSMYRLRSPDTNKPLFISHGIIQDYSENRVDTLHLKNLLHL
GEDRYLTTLVLKHFQDYKTKFVRHAYAKTVAPDSIKVLLSQRRRWINSTVHNLAELVFLD
QLCGFCCFSMRFVVFIDLLSTIIAPVTVAYIVYLIYLIVHDGSSIPTLSIVMLAAIYGLQ
AMIFIFRMRWDMIAWMIFYICAIPVFSFLLPLYSFWKMDDFSWGSTRLVVGDKGKKIVIH
DEGKFDPSSIPLRSWEEYENELWDQESVHSGSYMPPKAEYSYDYPRAQSTYSYGGHGYEQ
PVHPVQTRSTSPVSSRYQMSQFRQSPYQSPYQGPYGGSAVDFRPSRMDMAHQPSLDDTSS
FHQPYQPPPRPQSSYAFNLPDPSSDSFTAPAVDYLGAQAITDSQLERSIRKICANAELDK
LTKKGVRKELEREYGVELTERRETINRLVEKVLTE

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1196	1701	1.1e-236	0.9924098671726755

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
276845	MYSc_Myo17	0.0	16	738	31	647	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	1193	1701	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).
276950	MYSc	2.63e-132	18	729	29	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	4.55e-129	18	741	48	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.
276849	MYSc_Myo22	4.06e-110	16	728	27	660	class XXII myosin, motor domain. These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AAW44187.2|GT2	0.0	1	1895	1	1930
AUB26020.1|GT2	0.0	1	1895	1	1931
AFR96137.1|GT2	0.0	1	1895	1	1931
UOH81905.1|GT2	0.0	1	1895	1	1931
KGB75888.1|GT2	0.0	1	1895	1	1935

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7KCH_A	1.47e-62	61	742	121	734	Chain A, Unconventional myosin heavy chain [Chara corallina]
7DHW_A	1.15e-61	61	501	163	598	Chain A, Motor domain of myosin [Arabidopsis thaliana]
7R91_D	9.62e-61	13	737	39	675	Chain D, Isoform 3 of Unconventional myosin-XV [Mus musculus],7RB8_D Chain D, Isoform 3 of Unconventional myosin-XV [Mus musculus]
7B19_A	1.17e-60	2	745	88	779	Chain A, Myosin-2 heavy chain,Myosin-2 heavy chain [Dictyostelium discoideum]
2XEL_A	5.64e-60	2	745	76	766	Molecular Mechanism of Pentachloropseudilin Mediated Inhibition of Myosin Motor Activity [Dictyostelium discoideum],4AE3_A Crystal structure of ammosamide 272:myosin-2 motor domain complex [Dictyostelium discoideum AX4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4P9K9|CHS8_USTMA	0.0	25	1895	56	2004	Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
sp|J9VNT4|CHS5_CRYNH	0.0	1	1895	1	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	5.68e-286	831	1708	33	900	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VF17|CHS4_CRYNH	4.31e-273	744	1715	35	1005	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	4.95e-138	1220	1712	686	1195	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
1.000011	0.000051

TMHMM  Annotations     

Start	End
876	898
911	933
1179	1201
1572	1594
1604	1626
1633	1655