CAZyme Information: KGB75888.1

Basic Information

• Species: Cryptococcus gattii VGII
• Lineage: Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus gattii VGII
• CAZyme ID: KGB75888.1
• CAZy Family: GH128
• CAZyme Description: chitin synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1935		218353.86	6.7299

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CgattiiVGIIR265	6705	294750	281	6424

• Gene Location: location=CP025763:880037-886471(-)

Full Sequence      

MAQQPPPSRFQGVTDLSSLAVTEDTILVTLQERYLSHKPYTSLSPAALVFLSPYSYLPID
GEESLLRYVEEYYQSSNEEGGSRNEQGWWKKKLEEPHVFQLALSAYYNMRRTGQDQVIIA
SGPTGSGKTELKRLAIEAITQVSLANPGKKGSKIGVQVSSAEFILKCFGNAHTLSSDEAS
RFGTYTELQFNERGRLEGLKTIVYYFERSRVSQAPINGERNFHAFYYLVSGAPEEERSFL
KLGDVSDYRYLNCRVRRVGVDDRYRYSQLKQAFRMVGISNRLIAQIFQLLASILHIGNLR
FSPSDGTQEGASVINIDTLDIVAEFLGVHSESLAEIFSLKTVLIGKEVCTTFLGPEQAEQ
VRDELARTLYSLLFSWINEHINSKLCKDGFGSFIALVDLPGIQRNSGSMGSFNSVDQFCL
NFAAEKMHNWVLHRIHETTRQEAETERLLISRVPYFDNSECLGMLSNPRGGLISVIDDLS
QKKRSESNLLESLGKRFHNNPSISISPQGTRSSASFTINHYDGPVTYSTSNFLERNANET
STDIIQLLRGNTTSRSQVSTAEGHGSSNPFIKGLFGMKNIAMQTHPRSDSTIVAAQQSVR
PVRAPSTRRKKMTALGPVSEEGGEEACDFQVGGGNDESYSPKELHCIAGQHWAAVDSLLK
SFDQTQTWYIFTLRPNDSQLPSQFDLRSMKQQVRSFGIVEMAQQLQTSWEVRLSHKEACE
RYNEELLYRGIPEGTGDVERLRDLKRLMSLTDADMGIGFQRVFLSHSLFHFLEDRLRVKE
PGEQQAFEDLGHKKLQTDPFSPHRYQAASFDSQDHVHNDPPIRPVDSSANLPLMEHAQPN
VNNSLEIDDRESSAVPYVSYGGRSITDIEGYASSRDLLASPIHKSEKDPLDTEPQAGETT
EEYRESIARRRWVWLCSALTWWIPGFVLSKVAGMKRQDIRQAWREKLAINMIIWFICGCA
VFVIAILGPVICPTQHVYSTSELASHSYTLNPNNAFVAIRGEVFDLSQFAPIHLTAVSVV
PTKSIMQYGGLDASELLPVQVSALCGGVSGSVSQYVTLDSTNTTDVYSQYHDFRAYTNDS
RPDWYAEMMIMMRHRFRVGFMGYTKKDLKNMAGQGRAVAIYDNLVYDLSNYIQQNGGGLK
APNGVNLTAQDQADRQFMSDQVVSLFKYNSGKDITTLLDNLGSTIGTDVVERQKTCLRNL
FILGKLDTRDSAQCQFSTYILLALSCVMVAVIGFKFLSALHFGSVRAPESHDKFVICQVP
CYTEGEESLRRTIDSLCKLRYDDKRKLIFVICDGNIKGFGNDKPTPAIVLDILGVDVNND
PEPLSFQSLGEGAKQHNMGKVYAGLYECAGHVVPYLVIAKVGKPNERQKPGNRGKRDSQM
LVMHFLNKVHFNAPMNPLELEMYHQIKNVIGVNPSFYEYLFMIDADTTVDEMSLNRLVSA
MRHDKKIIGVCGETSIANAKQSIVTMSQVYEYFISHHLAKAFESLFGSITCLPGCFSMYR
LRSPDTNKPLFISNGIIQDYSENRVDTLHLKNLLHLGEDRYLTTLVLKHFQDYKTKFVRH
AYAKTVAPDSIKVLLSQRRRWINSTVHNLAELVFLDQLCGFCCFSMRFVVFIDLLSTIIA
PVTVAYIVYLIYLIIHDGASIPTLSIIMLAAIYGLQAMIFIFRMRWDMIAWMVFYICAIP
VFSFLLPLYSFWKMDDFSWGSTRLVVGDKGKKIVIHDEGKFDPSSIPLRSWEEYENELWD
QESIHSGSYMPPKAEYSYDYPRTQSTYSYSGYGYDQPTHPMQTRSISPVSSHYQMSQFRQ
SPYQSPYHSPYQGPYGGSIAEFRSSRMDMANRPSLDDTSSFHQLYQPPPRPQSSYALNLP
DPSSDSFTAPPVDYLGAQAITDGQLESSIRKICANAELDKLTKKGVRKELEKEYGVELTE
RREIINRLVEKILTE

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1232	1737	6.5e-237	0.9924098671726755

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
276845	MYSc_Myo17	0.0	21	774	1	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	1229	1737	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	1.03e-137	24	765	1	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	1.87e-135	7	777	2	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	1.79e-110	25	764	2	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
KGB75888.1|GT2	0.0	1	1935	1	1935
ADV23055.1|GT2	0.0	1	1935	1	1935
AAW44187.2|GT2	0.0	1	1935	1	1930
AUB26020.1|GT2	0.0	1	1935	1	1931
AFR96137.1|GT2	0.0	1	1935	1	1931

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5HMP_A	3.51e-62	7	722	59	695	Myosin Vc pre-powerstroke state [Homo sapiens],5HMP_B Myosin Vc pre-powerstroke state [Homo sapiens]
4ZG4_B	4.38e-62	7	722	63	699	Myosin Vc Pre-powerstroke [Homo sapiens],4ZG4_E Myosin Vc Pre-powerstroke [Homo sapiens]
7R91_D	1.33e-60	12	779	3	682	Chain D, Isoform 3 of Unconventional myosin-XV [Mus musculus],7RB8_D Chain D, Isoform 3 of Unconventional myosin-XV [Mus musculus]
7B19_A	3.91e-60	2	781	88	779	Chain A, Myosin-2 heavy chain,Myosin-2 heavy chain [Dictyostelium discoideum]
7RB9_D	7.93e-60	12	779	3	682	Chain D, Isoform 3 of Unconventional myosin-XV [Mus musculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4P9K9|CHS8_USTMA	0.0	8	1935	2	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	1935	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	2.39e-288	867	1743	33	899	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VF17|CHS4_CRYNH	3.82e-274	780	1791	35	1034	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	2.45e-137	1256	1748	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
1.000067	0.000000

TMHMM  Annotations     

Start	End
912	934
947	969
1215	1237
1614	1636
1640	1662
1669	1691