CAZyme Information: AMAG_09745-t26_1-p1

Basic Information

• Species: Allomyces macrogynus
• Lineage: Blastocladiomycota; Blastocladiomycetes; ; Blastocladiaceae; Allomyces; Allomyces macrogynus
• CAZyme ID: AMAG_09745-t26_1-p1
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1568	GG745348|CGC1	174242.63	6.5093

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AmacrogynusATCC38327	19333	578462	535	18798

• Gene Location: location=GG745348:602752-608502(-)

Full Sequence      

MDQAAPLADALHAALANASASRGTTLGGYAVRPLTDETDPAVDDAIDDLDAAIAATLYGG
YNNSQLYTRLGTSALVAVAPPAMSTILAELTSEQMKDRWYKQYKNLKAEPLPSAIAAGRA
PHNAGSAASLTPHVFGLANSLYFHLRRSGVDQSVVLRGESGSSKSLQAELLLQQLCAISG
NSKRDEKVHRRVLAAQTVLAAFGAAKTATSNDASRFGAYYEVQFSDRGKMVGLKLITYGL
ERDRVAKQRLGERNFHVFYYLLAAASPEQKQAFGLLGSQNGQAGTVFPYLNYGALPTQGI
DDAGRFEALQDAMRAVGISKRVQHYMFKLLAAILHLGNISFANDQFHEQDNCVVRNREAL
QFVADLLEVDARFLESALTSRTHLVGRDLVTALLTAEKAAENRDNLAKVLYNVLFMYLVE
AINKKLCSDEDMANFIAILDFPGNVATKTSSGANGGSSAAKNAAAEDYGAAGVAYAYCNE
RLDAFINKRLFEPRSSRGATPKRHRPRFNAFAADARTEYSAENDSVYSDGDYTDDGFGTE
YDGDSVYDDSIAGGPAGSGTGEGGALTERQLKARTEATKGDPLLDMDNAQVEEYTLTPQR
KRWIFATWFLTWWIPTPFLRWCGGMQRDDIRMAWREKCAIFILIMFMCAVQLFFIIGFGR
LICPRQNILNLNELYYKTGGGTENPEALVGIYGAIYDLNNFYDTPYHAKDIMGSYAGYDV
TAGFPRTPAFYCSYARESAPNFPPMFSRSTVANGTFIQLRHQEFYERDMYGAQRKIDWKL
RQNVKSLVGWDPDDVEALSQKSLNPRLLIIVKDRVYDLQPYVNAAVGQAFLPPDIVEFIK
QNRGTDLTSNPSFMGVWRREPQLRNCFNNLFVVGVVDYRKSGRCMFTNYILVAFSVLLAL
VIGAKFLAALQLGSAGTPEEHDKFVMLQVPCYTEGEESLRTTIDSLASMSYDDKRKLLFI
ICDGNIMGSGNDRPTPRIVLDILGVDPTVDPEPLSFQSIGEGMKQHNMGKVYAGLYECSG
HLVPYLVVVKVGKPSESSKPGNRGKRDSQMILMRFLNKVYFDSPMSPLELEMYHQIKNVI
GVNPAFYELMLCVDSDTKVHQDSLTRLVSVMTHDTKVIGCCGETRLANEKDSWATMIQVY
EYYISHHMAKAFESLFGSVTCLPGCFSMYRLRSATKSRPLLVSNELIADYGDCNVDTLHK
KNLLSLGEDRYLTTLLLKHFPNMRTVFTADARCETDAPERWEVLLSQRRRWINSTIHNLV
ELLSISQLCGFCCFSMRFVVLIDLVATFLQPAIVAYLGYLIYLVVVSITSHDQNAFPMIS
LILLGIIYGLQAIIFLIKREWQHVGWMFIYILAIPIFSFFIPVYSFWKMDDFSWGNTRIV
VGEAGKKQVMVAGDEAQRFDLRIIPHKRWSEYEADLWDQEGDLYSPQHPEDDNRSVRSGY
SASGMSRSRSVASAAAAAAAAAAAAAADLKRSNSTATAGTNFSISQLYGAPGAPPVPALP
AHLGFPTDDEIYAEVQRMLATANLMTITKKQVRDELSALFNVDLTPRKDFINQCINEVLQ
QQTQNMHM

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	903	1414	7.2e-236	0.9886148007590133

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
367353	Chitin_synth_2	0.0	902	1415	4	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	1.46e-127	64	492	17	409	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	1.47e-94	61	443	30	378	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	3.66e-88	61	443	11	372	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.
276829	MYSc_Myo1	5.99e-77	130	440	52	359	class I myosin, motor domain. Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. 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
CCA72950.1|GT2	0.0	53	1559	21	1903
CDS06114.1|GT2	0.0	50	1560	22	1892
QRV98874.1|GT2	0.0	50	1555	26	1903
CDS08031.1|GT2	0.0	52	1416	24	1689
CDS05327.1|GT2	0.0	35	1418	16	1714

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1LVK_A	4.46e-53	130	492	151	488	X-Ray Crystal Structure Of The Mg (Dot) 2'(3')-O-(N- Methylanthraniloyl) Nucleotide Bound To Dictyostelium Discoideum Myosin Motor Domain [Dictyostelium discoideum]
1MMG_A	7.98e-53	130	492	151	488	X-Ray Structures Of The Mgadp, Mgatpgammas, And Mgamppnp Complexes Of The Dictyostelium Discoideum Myosin Motor Domain [Dictyostelium discoideum]
1MMN_A	1.07e-52	130	492	151	488	X-Ray Structures Of The Mgadp, Mgatpgammas, And Mgamppnp Complexes Of The Dictyostelium Discoideum Myosin Motor Domain [Dictyostelium discoideum]
1MMD_A	1.43e-52	130	492	151	488	Truncated Head Of Myosin From Dictyostelium Discoideum Complexed With Mgadp-Bef3 [Dictyostelium discoideum],1MND_A Truncated Head Of Myosin From Dictyostelium Discoideum Complexed With Mgadp-Alf4 [Dictyostelium discoideum],1MNE_A Truncated Head Of Myosin From Dictyostelium Discoideum Complexed With Mg-Pyrophosphate [Dictyostelium discoideum],1VOM_A Complex Between Dictyostelium Myosin And Mgadp And Vanadate At 1.9a Resolution [Dictyostelium discoideum]
3MYH_X	1.91e-52	130	492	151	488	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VNT4|CHS5_CRYNH	3.53e-294	132	1559	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|Q4P9K9|CHS8_USTMA	6.19e-287	67	1419	35	1753	Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
sp|O13395|CHS6_USTMA	6.84e-286	591	1420	61	898	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VF17|CHS4_CRYNH	8.03e-274	568	1441	123	1018	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|Q4P333|CHS7_USTMA	1.92e-148	603	1413	83	951	Chitin synthase 7 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS7 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000056	0.000001

TMHMM  Annotations     

Start	End
640	662
888	910
1259	1281
1288	1310
1315	1337
1344	1366