CAZyme Information: ASPSYDRAFT_151574-t33_1-p1

Basic Information

• Species: Aspergillus sydowii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus sydowii
• CAZyme ID: ASPSYDRAFT_151574-t33_1-p1
• CAZy Family: AA9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1855	KV878586|CGC9	206787.94	7.2509

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsydowiiCBS593.65	13717	1036612	138	13579

• Gene Location: location=KV878586:1705922-1711667(-)

Full Sequence      

MAGTSPAGHTPSHVQSSLPSLPAHLQSDTHLTAHLASRFHVGLPTARLSSHALISLNNYT
SSSKGPDGGKDGSAMGEAEDLAKRAYTRLGTRGENQAVVFLGESGSGKTTLRSHLLSSFL
SYSSTPLSSKLSYAAFIFDTLTTTKSLTTPTASKAGLFLELQYDGSSAVHPTLIGGKIIE
HRLERSRIASVPTGERSFHALYYLLAGTSAAEKSHLGLDSSIHVTTAGGRLTSADHKRWR
YLGHPTQLKVGINDADGFQHFKTALRKLEFPRSDIAEICQILAAILHIGQLDFGSGQATM
TGAEESGGYSHEGGETVTVVKNKDVLSIVAAFLGLGLGELETSFGYRTKTIHRERVTVML
DPKGARRNADELSRVLYSLLVAYVIENVNQRICAAEDSVANTVSIIDFPGFSQVCSTGST
LDQLLNNAAIESLYNFCLRSFFDRKADMLEREEVAVPATSYFDNTDAVRGLLKQGNGLLS
ILDDQTRRGRTDAQFVEAVRRRFENKNTAINAGSTGAESGYGMVSQNARSSFTVKHFAGE
VDYSATGLLEENGEVISGDLMNLMKSTRSDFVKELFGQEALQTVAHPKERSAIMQAQVSS
KPTRMPSMARRKASPPSRLTFDAAVAEDPYESESQAGSSAKNSSAKRRSGMLMGGMQGAA
GQFLSSLDIVNKCLTANNLNPYFVFCLKPNDRRIANQFDSKCVRAQVQTLGIAEISQRLR
NADFSIFLPFAEFLGLAEVGNIVVGSDKEKSEVVLDEKRWPGNEARVGSTGVFLSERCWA
DLAKVGERVIPSYGLEDDGGDALLHPRSANYADSKVRLLNSVDHSPGAYIYGDESKQGSN
ASRDFDGRSEAGFSAFNSGDMFRNLETREQMLEKGNEKEMEEVDELTVSGSRKRWMALVW
FLTWYIPTPAIRFIGRMKRKDVQVAWREKFAINLLIWLCCGIAIFIIVGFPALICPTQHV
YSASELSSHDGEDGNSAFTSIRGLVLDLGEFMPRHYPNIVPESALKKYAGKDSTGLFPVQ
VSALCAGKDGKVDPKVLLNYEPTNFTGSVQTVGSGDPNSLYHDFRWFRKGGDYRPDWYIE
QMRVLKSNYYKGWVGYSSQYMKTLADKDQNIASINGKVYDLTTYIAGGRRIQGREGEDIS
GVDSDFMDPLVVDLFQQKPGQDITKLWENLQINPKLRTDMMKCLDNLFIVGHVDTRNSTQ
CQFARYFILAISILICSVVIFKFFAALQFGKKNLPENLDKFIICQVPAYTEDEESLRRAI
DSMARMRYDDKRKLLVIICDGMIIGQGNDRPTPRIVLDILGVPETVDPEPLSFESLGEGM
KQHNMGKVYSGLYEVQGHIVPFLVVVKVGKPSEVSRPGNRGKRDSQMVLMRFLNRVHYNL
PMSPMELEIHHQIRNIIGVNPTFYEFILQVDADTVVAQDAATRMVSSCLNDVRIIGVCGE
TSLTNAKTSAVTMIQVYEYYISHNLTKAFESLFGSVTCLPGCFTMYRIRSAESGKPLFVS
KEVVESYSEIRVDTLHMKNLLHLGEDRYLTTLLLKHHPKFKTKYIFRAQAWTIAPESWAV
FLSQRRRWINSTVHNLVELIPLQQLCGFCCFSMRFVVFIDLISTIIMPVTIAYIIYLIVW
LARDTSTIPWTSFLLLAAIYGLQAIIFIMRRKWEMIGWMIIYILAMPVYALALPLYSFWH
MDDFSWGNTRVITGEKGRKVVISDEGKFDPETIPKKRWEEYQAELWDVQTSRDDRSEISG
ISYGTKYHPTAQSEYGIPGSRPMSQLDMPRHMSRMSLAPSEMMSRHMDMEMEDISHLPNE
DAILSEIRDILRTADLMTVTKKNIKQELERRFGVNLDTKRPYINSATEAVLSGNL

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1217	1724	1.2e-244	0.9962049335863378

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
276845	MYSc_Myo17	0.0	26	782	1	645	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	1216	1724	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).
214580	MYSc	2.11e-169	6	787	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.
276950	MYSc	1.03e-79	81	775	60	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.
133033	Chitin_synth_C	8.74e-70	1243	1575	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS26571.1|GT2	0.0	1	1855	1	1855
BAA21714.1|GT2|2.4.1.16	0.0	1	1855	1	1852
EAA58702.1|GT2	0.0	1	1855	1	1852
QMW30181.1|GT2	0.0	1	1855	1	1857
QMW42253.1|GT2	0.0	1	1855	1	1857

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4A7F_C	1.39e-42	81	774	80	679	Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 3) [Dictyostelium discoideum],4A7F_G Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 3) [Dictyostelium discoideum],4A7F_J Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 3) [Dictyostelium discoideum],4A7H_C Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 2) [Dictyostelium discoideum],4A7H_I Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 2) [Dictyostelium discoideum],4A7H_J Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 2) [Dictyostelium discoideum],4A7L_C Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 1) [Dictyostelium discoideum],4A7L_G Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 1) [Dictyostelium discoideum],4A7L_J Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 1) [Dictyostelium discoideum]
5I0H_A	3.82e-42	81	784	136	736	Crystal structure of myosin X motor domain in pre-powerstroke state [Homo sapiens],5I0H_B Crystal structure of myosin X motor domain in pre-powerstroke state [Homo sapiens]
5I0I_A	4.37e-42	81	790	134	740	Crystal structure of myosin X motor domain with 2IQ motifs in pre-powerstroke state [Homo sapiens],5I0I_B Crystal structure of myosin X motor domain with 2IQ motifs in pre-powerstroke state [Homo sapiens]
1LKX_A	5.88e-42	81	774	80	679	Motor Domain Of Myoe, A Class-i Myosin [Dictyostelium discoideum],1LKX_B Motor Domain Of Myoe, A Class-i Myosin [Dictyostelium discoideum],1LKX_C Motor Domain Of Myoe, A Class-i Myosin [Dictyostelium discoideum],1LKX_D Motor Domain Of Myoe, A Class-i Myosin [Dictyostelium discoideum]
5KG8_A	8.87e-42	81	784	134	734	Rigor myosin X co-complexed with an actin filament [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4P9K9|CHS8_USTMA	0.0	35	1758	25	1789	Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
sp|J9VNT4|CHS5_CRYNH	0.0	81	1852	101	1930	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	1.24e-284	883	1742	61	912	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VF17|CHS4_CRYNH	1.35e-266	877	1777	148	1053	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	4.78e-129	895	1748	75	980	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
1.000050	0.000000

TMHMM  Annotations     

Start	End
896	915
932	954
1203	1225
1595	1617
1627	1649
1656	1678