CAZyme Information: OON06442.1

Basic Information

• Species: Batrachochytrium salamandrivorans
• Lineage: Chytridiomycota; Chytridiomycetes; ; NA; Batrachochytrium; Batrachochytrium salamandrivorans
• CAZyme ID: OON06442.1
• CAZy Family: GT2
• CAZyme Description: Chitin synthase [Source:UniProtKB/TrEMBL;Acc:A0A1S8VWA0]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1855		207526.29	7.1065

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_BsalamandrivoransBS	10186	N/A	51	10135

• Gene Location: location=LYON01000572:1920-8123(-)

Full Sequence      

MGDTNVQDLVDLPSATADEVAKYLREQAARCQPFVRIGSRAMAVINIPQALTYDEKTSEN
YGSPVTGNGDISVAVAAAPHIYDLVTKVFMNMMGKHTDQSIVLCGSEISGKSLCTRMISR
HICSLSLNASKKSRMISGVTKMETVLSMFGCAATSANTLVARFGRYTEYQFDDRGKMIGV
KLLDYLFDRDRVVSVPSLESNFDIFYCLLSGATEQERIEWHLSDASSFSYLNRAGKLITG
PTSSVLRERFDELRQHLKSLGIGARTQSLLFRTIVAILYLGEIEFENTAGPNEPCLVKNR
DILDIVANMLGVGPDHLEYALTFQTKPVFKEMCTVFLSDQGAKQQRNEISKILYSLLFRW
IIEHLNTRLCTEDSETCIGILDFVSFTKGKEDHNDFHTFMVNIANERLAAYSRRGYAHIL
VELYNEGLVNINPSMLNPAKTATAVELAWSPDSNSILSIINTESQKFAGDRSAAELKTAQ
KMHDMCSPNLLYTPMGRTEFKINHYVEPVVYDLSGFTECNRSMIGPDVIALFRGSSTLAI
PASTNLFVRNLFIEANVATSRLARSDDVIASGYQSGIPKRCTSTYMRNHPKTATEAPQDE
TKDTHSHREAISRPALQSKGAFSGQDQQQRIPLCTMDLDVSLTELEETLDSTEIWTLFCI
SLNRTVGPIDWKYMSSQVKSMDIPRLIEIAKHSTSFAHSYTFNEFVDAYRPVIVQLVPSL
NVSGYTNEMLCDAAVSHMAMCGNQGIRQGPNKIFLSDTAWGQFEDAKSTGTPISVNEIAG
FPGMDRGTRRRMSAKTQGSGQDDDMLSEFTSVSRSRRPRSPAYTADQSNSDDVTFDLGPD
PVQSERDGSDKRDRDEDSLDGLQHPKNRMSKQRCQWMCCTWMLTWWIPSFVLLYCCGMKR
PDIRMAWREKVALCIIIFLMCCALLFFIIGFGRLLCPKQQVLSTFELASKSSISDPWVYA
NGRVYQISDILANHLNSYGIPNFQFSSFLGGDVSSLFFAGQNFVQYCPGLPPPQAGWDPI
SSRPKSDSTHYPHVAIDPKTGTQKLYLEFMNKYAKARLGFTPEFISKMASTERRLIIIHD
NVYDVSGYFNADSRFLGPMVEQLFGNFYGKDATAQWSQIQQVDPNANLYMRCMNNMFYIG
TVDHRNDFKCQFSNYMLLATSVILVSVVGFKFLAALRFGSSRDPEFHDKFVICQVPCYTE
GAESLEKTLESLAIMQYDDRRKLLFVIADGMIVGSGNDRPTPQIVLDILGVDPNATIDTE
SFSFQSLGDGDMQHNKGKVYSGLYKVQGHSVPFVVVVKTGKSSERRRPGNRGKRDSQLIL
MRFLSRVHFNAEMAPLELEIFHHMKNIIGVHPSFYEYVLMVDADTEVYPDALNKLVSTMM
HDSKIMGLCGETLLSNEKDSWITMIQVYEYFISHHLSKAFESMFGSVTCLPGCFSMYRIR
TPTKAVPLLIAPGIVADYSQNSVDTLHLKNLLHLGEDRYLTTLMMKHFPNLKLSFNPDAQ
CRTNAPDQWKVLLSQRRRWINSTVHNLVELLSLEQMCGFCCFSMRFVVFLDLFSTVVQPA
GVLYIGYLIYSLITSSDVFPTISIVMLAAIYGFQVIIFVFKRQWAQIGWMIVYILATPVF
GFYIPLYSFWRFDDFSWGNTRVVVGDLAGSGKLTTKKFDPESIALRRWADSDYDKWEGQS
QISGNLSSSGGTPGSAGIMKSSYGLTVTIPKASSTTGMQGNTSAPSYGATQVLETAKSPI
QINSAGTSSSYATSIRGRSTGREALLQPVPAHLPPVVNNPTSQGARFPQQTTPRPTSPSD
SDIIRELRGILATVDLMVVTKREVRDRVCQRLGVDLSSRRGEISALMDQILQGKI

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1167	1670	5.7e-231	0.9867172675521821

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
367353	Chitin_synth_2	0.0	1165	1670	1	523	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).
276845	MYSc_Myo17	1.07e-133	28	765	11	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.
214580	MYSc	4.62e-88	78	564	72	543	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.
133033	Chitin_synth_C	2.06e-76	1306	1526	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.
276950	MYSc	3.48e-74	53	536	36	517	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS08031.1|GT2	0.0	5	1668	10	1682
QRV98874.1|GT2	0.0	5	1854	13	1910
CDS06114.1|GT2	0.0	5	1853	10	1893
AZQ26801.1|GT2	0.0	5	1851	14	1906
QDK64613.1|GT2	0.0	5	1851	14	1906

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3MKD_A	1.10e-49	78	559	151	618	Crystal structure of myosin-2 dictyostelium discoideum motor domain S456Y mutant in complex with adp-orthovanadate [Dictyostelium discoideum]
1FMV_A	1.96e-49	78	559	152	619	CRYSTAL STRUCTURE OF THE APO MOTOR DOMAIN OF DICTYOSTELLIUM MYOSIN II [Dictyostelium discoideum],1FMW_A Crystal Structure Of The Mgatp Complex For The Motor Domain Of Dictyostelium Myosin Ii [Dictyostelium discoideum]
3MYH_X	1.98e-49	78	559	152	619	Insights into the Importance of Hydrogen Bonding in the Gamma-Phosphate Binding Pocket of Myosin: Structural and Functional Studies of Ser236 [Dictyostelium discoideum],3MYK_X Insights into the Importance of Hydrogen Bonding in the Gamma-Phosphate Binding Pocket of Myosin: Structural and Functional Studies of Ser236 [Dictyostelium discoideum],3MYL_X Insights into the Importance of Hydrogen Bonding in the Gamma-Phosphate Binding Pocket of Myosin: Structural and Functional Studies of Ser236 [Dictyostelium discoideum]
1MMN_A	1.98e-49	78	559	152	619	X-Ray Structures Of The Mgadp, Mgatpgammas, And Mgamppnp Complexes Of The Dictyostelium Discoideum Myosin Motor Domain [Dictyostelium discoideum]
1D0X_A	2.61e-49	78	559	152	619	Chain A, MYOSIN S1DC MOTOR DOMAIN [Dictyostelium discoideum],1D0Y_A Chain A, MYOSIN S1DC MOTOR DOMAIN [Dictyostelium discoideum],1D0Z_A Chain A, MYOSIN [Dictyostelium discoideum],1D1A_A Chain A, MYOSIN [Dictyostelium discoideum],1D1B_A Chain A, MYOSIN [Dictyostelium discoideum],1D1C_A Chain A, 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	6	1851	7	2002	Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
sp|J9VNT4|CHS5_CRYNH	0.0	79	1851	96	1929	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	6.16e-263	876	1677	73	896	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VF17|CHS4_CRYNH	7.46e-244	821	1680	116	997	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|O13356|CHS1_CRYNH	2.67e-144	876	1670	75	952	Chitin synthase 1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=CHS1 PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000052	0.000000

TMHMM  Annotations     

Start	End
876	898
911	933
1157	1179
1546	1568
1578	1600
1607	1629