CAZyme Information: I317_04348-t43_1-p1

Basic Information

• Species: Kwoniella heveanensis
• Lineage: Basidiomycota; Tremellomycetes; ; Cryptococcaceae; Kwoniella; Kwoniella heveanensis
• CAZyme ID: I317_04348-t43_1-p1
• CAZy Family: GH43|CBM91|CBM67|GH78
• CAZyme Description: chitin synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2070	KV700203|CGC1	231184.39	6.4488

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_KheveanensisCBS569	8002	1296119	131	7871

• Gene Location: location=KV700203:81555-88748(-)

Full Sequence      

MSAGYSTPGPSSRGGGRGGGVGGFGPSRFEGIQDLCNLSSIAEDTVIVTLRERYLSAQPY
TALSPSAIVSVNPHTYLPVNGDASLQDYVAEYYKITTDDTTSRSQSRGDDSPIGGRDKDR
LGPHIFQLALSAYYNMRRTRQDQIVVTSGPVASGKSEMKRLAIKAISEVSVAAPGKKGAK
IGSQIANAEFILESFGNAHTLGNDNASRFGNYTELQFNDRGRLEGLKTIEYYFERSRVSQ
TPFSGERNFHVFYYLVSGVHGEEKSFLKLEEPSSYRYLQSRVRRTGMDDRQRFEQLKQAF
RVVGLSNRLVAQVCQLLATILHIGNLQFESGNGVQQEGAVASNFDTLATVAEFLGVSSEA
LAELFSFKTVLMRKEVCTTFLDAEQAEGVRDELARTLYSLLFSWLNEHINQKLCKDSFGS
FIALLDLPGIQNNSGPVAMSNSVDQFCFNFANEKLHNWLLHRIHEVPLEEATKEKLTATR
LPYFDNSECLRMLSDAKGGMIYIMDDMSRKKRNEAQFLEAMGKRFNGHASFSLAANSRSG
AASFTVNHYDGPVAYNTENFLERNANETSADILRLLRGNTSGASAPSDHQGSNNPFIKSL
FSNKSIATQTHPRNDDEIVAVQQPVRPMRAPSTRRRKGRPLRAVTEEDEDDEGEDDEVGG
GNEGGNAGKSLHCIAGQHWAALDTLLQTFDQAQPWFVFCLRPNDSQLPSQVEIKSVKAQI
RSMGLTEMAQRMQTFYEVRMSHFEACDRYAEEFQVRGIPEGPSDVDRLQDLKRVLKLGDS
QMAIGANRVFLSHAVFRRFEDRLRADEKDEQKHKRGGEDMEYLDEKDHKLDPFSPYHRDV
SPAASPAMGYTDPYLQNESTAALPLVEHAQPLRQDSPDEFDDIRGFAPSQITSQYGDSAS
AVGTETYAPSRNMFRDFDHKDEKDPLDAEPQDGETTEEYKESIARRRWVWLCMLLTFWIP
GFVLNKIGGMKRQDIRQAWREKLAINMIIWFICGCTVFVVAFLGPLICPTQHVYTFGELA
SHSYKNDPNNAFVAIRGEVFDLSQFAPTHLTAVSVVPQKALMQYGGLDASNLFPVQVSAL
CGGTTGSISPYVTLDSTNTTDPFMQYHDFRAFTNDSRPDWYAEMMIMMRHRFRVGFMGYT
KKDIKKMANSGRAVAIYDGLVYEMTTYIQQNGGGLRSPDGVNLTADDQNARRFMSDQVIE
LFTYNAGKDITKLLDDLSNSIGEDVVDRQKVCLRNLFIIGKVDSRDSAQCQFSTYILLAL
SIVMVSIIGFKFLAALHFGSSRAPENHDKFVICQVPCYTEGEESLRRTIDSLVRLKYDDK
RKLLLVVCDGNIKGYGNDKSTPQIVRDILGVDPNADPEPLSFQSLGEGAKQHNMGKIYAG
LYECAGHVVPYLVVVKVGKPTERPKPGNRGKRDSQMIVMHFLNKVHFNAPMNPLELEMYH
QIKNVIGVNPSFYEYLFMVDADTTVDELSLNRLVSAMMHDKKIIGVCGETSIANSKQSIV
TMSQVYEYFISHHLAKAFESLFGSITCLPGCFSMYRLRSPDTHKPLFISNAIIQDYSENR
VDTLHLKNLLHLGEDRYLTTLVLKHFNDYKTKFVRDAYAQTVAPDSAKVLLSQRRRWINS
TVHNLAELVFLDQLCGFCCFSMRFVVFIDLISTIVAPVSVAYIVYLIYLVAGEGKGIPAL
SIIMLAAIYGLQALVFIFRLRWDMVAWMVFYILAIPVFSFFLPLYSFWKMDDFSWGSTRL
VVGEKGKKIVIHDEGKFDPRSIPLKSWNDYENELWDQESQHSESYLPDMKGEYESRPGSA
YGYDGGFDGRSRGLSPANSYGDLRGQSRGGSVYGGVPQLPYSSQGHGDMLMGDNRSMYDN
KSFYGGNGGGGADTRSLYANSFYGQPALENRGSSYSLSGAPHMGYGQQGMGVPQMNMTMG
MSPNMMGLDHRVSSYSSFNPPASNQHYPPEQMMQHRPSPLSNPASRPTSNFLGDLPLSST
EGGGGGISLGAQGITDAQLEVSIRRICGEADLDTLTKKTVRKQLEEEYGTPLGGRKDAIN
RIIEQVLAGEWMDTTTLLSRLRCRGVLEVS

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1266	1773	1.1e-236	0.9962049335863378

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
367353	Chitin_synth_2	0.0	1265	1773	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).
276845	MYSc_Myo17	0.0	41	801	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.
214580	MYSc	8.00e-147	29	804	5	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	2.57e-145	44	792	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.
276849	MYSc_Myo22	6.97e-119	45	791	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
CCM73232.1|GT2	0.0	25	2051	18	2059
AAW44187.2|GT2	0.0	26	2047	7	1928
KGB75888.1|GT2	0.0	26	2047	7	1933
AUB26020.1|GT2	0.0	26	2047	7	1929
AFR96137.1|GT2	0.0	26	2047	7	1929

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1W9K_A	1.18e-75	26	810	82	767	Dictyostelium discoideum Myosin II motor domain S456E with bound MgADP-BeFx [Dictyostelium discoideum]
1W9L_A	1.59e-75	26	810	82	767	Myosin II Dictyostelium discoideum motor domain S456E bound with MgADP-AlF4 [Dictyostelium discoideum]
1MMG_A	1.84e-75	26	801	82	756	X-Ray Structures Of The Mgadp, Mgatpgammas, And Mgamppnp Complexes Of The Dictyostelium Discoideum Myosin Motor Domain [Dictyostelium discoideum]
1MMN_A	1.84e-75	26	801	82	756	X-Ray Structures Of The Mgadp, Mgatpgammas, And Mgamppnp Complexes Of The Dictyostelium Discoideum Myosin Motor Domain [Dictyostelium discoideum]
1W9I_A	2.14e-75	26	810	82	767	Myosin II Dictyostelium discoideum motor domain S456Y bound with MgADP-BeFx [Dictyostelium discoideum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VNT4|CHS5_CRYNH	0.0	26	2047	7	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|Q4P9K9|CHS8_USTMA	0.0	27	2048	2	2003	Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
sp|O13395|CHS6_USTMA	8.06e-278	922	1779	49	899	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VF17|CHS4_CRYNH	1.10e-262	909	1801	116	1019	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	2.29e-132	1292	1781	686	1192	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
1.000019	0.000015

TMHMM  Annotations     

Start	End
948	970
983	1005
1254	1276
1644	1666
1676	1698
1705	1727