CAZyme Information: TREMEDRAFT_74136-t26_1-p1

Basic Information

• Species: Tremella mesenterica
• Lineage: Basidiomycota; Tremellomycetes; ; Tremellaceae; Tremella; Tremella mesenterica
• CAZyme ID: TREMEDRAFT_74136-t26_1-p1
• CAZy Family: GT90
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1963	JH711534|CGC5	219890.38	6.8308

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TmesentericaDSM1558	8309	578456	1	8308

• Gene Location: location=JH711534:597214-604837(-)

Full Sequence      

MSEASKRFTSRFELTTDLCALPSVAEDTIVATLRERYLASQPYTALSSSALVSVNPLTYL
PVNGDAPLQDYVAEYHRNAVEDASGNKERLGPHIFRLALSAYYNMRRTRQDQIMVLNGAS
GSGKTEMRRLAVKAISEVSVASPGRKGAKVGPQVANAEFILESFGNAHTLSNDNASRFGN
YTELQFNDRGRLEGLKTIEYYFERSRVSQPPATGERNFHVFYYLVSGIVGEEKSFLKLGH
VNDYHYLRGRVRRTGVSDEQRFEQLKQAFRAVGLSTRLVAQVCQLLAAILHIGNLQFSGD
RSMHEGAIVDNLDVLNTVAEFLGIHADLLAELFSFKTLLIRKEVCTTFLDPQQAEDVRDE
LARTLYSLLFSWLNEHINQKLCRDSFGSFIALLDLPGPQNNAGLTSAVNSVDQFCFNFAN
EKLQNWTLHRLHEVPFEEASRERLPISRLPYYDNSECLKMLADPKGGVIHIMDDQARKKK
SEASFLEALGKRHTVHASFSLGDTSRQAGSSFTINHYSGAVTYSTENFLERNANETSADI
LRLLKGTPGAVGEDQGSNNPFIKGLFSSKAMTTQAHPRNDDTIVAAQQPVRPMRAPSTRR
KKGPRLTAVTEEEEDDQVGGGNDEAPAGAEKEMQCVAGQHRAALDTLLGTFDQAQPWFAF
CVRPNDSQLPSQVETRSVKAQIRSIGLTEMAQRLQMCYEVRMSHAEACERYAEELTLNGV
DSEKTSAQQLHELKEKLGLKDLDMGIGTTTVFLSHSVFQRFEDRLRSQEPSERPKYTERE
NTSGDLKVDPFSPYSKDVSPIHSPALGQLPYSAQDSSVALPLVQYAQPLPQESLDDLDRT
RGFAPSQVASQYDTMSNVGTETYAPSRNMFRDMDHKDEKDVLDEEPQDGEITEEYRESAA
RRRWVLLCTMLTFWIPNFMLNKLGGMKRQDIRQAWREKLTINLIIWFICGCTVFVIAFLG
PIICPTQHVYSSSELASHSTKLNPNNAFVSIRGEVFDLSTFATTHLTAVSVVPTKSVLQY
GGLDASHLFPVQVNALCQGTTGSLSPWVTLDTTNTSDPYSQYHDFRAFTNDSRPDWYAEQ
MIMLRYRYRVGFMGYTKKDLKNMANAGRAVGVYNNLVYELTTYIQQNGGGLKTPNGVNLT
AQDQADRQFMSPEVVSLFTYNSGKDITTLLDNLSGTIGSDVVNNQKVCLRNLFIIGKLDT
RDSPQCQFSTYILLALSCIMVAIIGFKFLAAIHFSSSRAPEKPDKFVICQVPCYTEGEES
LRRTIDSLVRLEYDDKRKLLVIICDGNIKGYGNDKSTPGIVLDILGVEGHQDPEPLSFQS
LGEGAKQHNMGKIYAGLYETAGHIVPYLVVVKVGKPTERPKPGNRGKRDSQMILMHFLNK
VHFNAPMNPLELEMYHQIKNVIGVNPSFYEYIFMVDADTTVEKLSLNRLVAAMQHDKKII
GVCGETSISNAKQSIVTMSQVYEYFISHHLAKSFESLFGSITCLPGCFSMYRLRTPDTHK
PLFISNQIIQDYSENRVDTLHLKNLLHLGEDRYLTTLVLKHFPKYKTKFVRDAHAETVAP
DSSKVLLSQRRRWINSTVHNLAELVFLEQLCGFCCFSMRFVVFIDLLSTIVAPVTVAYIV
YLVYLVAHNHATIPTLSIVMLAAIYGLQALVFIFRLRWDMIAWMVFYILAIPVFSFFLPL
YSFWRMDDFSWGSTRLVVGEKGKKLVIHDEGKFDPRSIPLKSWNDYENELWDHESSHSHG
SFIPQKDHPFQDHTGNGYGYGSRAPSSYGGDNFEPPMRNMSHAGSYVDLRAASRPPSSYN
PLPHPGYAGSMTGSYHPPGNFDQRSFYAGSIYNQPPPPMIQMGQMGTMPPQGGTDRQSSY
SYFDPAQARGSSYSLSNQIQTSGQNQPSAGMLPEVAIPGLSLGQAGVTDGQLELSIRRIC
QGADLDKLTKKGVRKQLEEEYGCDFSERKDAIGKIIERVLVVA

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1223	1729	7.2e-239	0.9943074003795066

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
367353	Chitin_synth_2	0.0	1221	1729	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	24	763	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.
276950	MYSc	3.91e-160	27	754	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	9.16e-156	12	766	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.
276849	MYSc_Myo22	7.73e-127	28	753	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	9	1960	19	2055
KGB75888.1|GT2	0.0	10	1960	8	1933
AAW44187.2|GT2	0.0	10	1960	8	1928
AUB26020.1|GT2	0.0	10	1960	8	1929
AFR96137.1|GT2	0.0	10	1960	8	1929

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7B1A_A	6.57e-79	3	770	87	778	Chain A, Myosin-2 heavy chain [Dictyostelium discoideum]
2XEL_A	1.72e-78	3	770	75	766	Molecular Mechanism of Pentachloropseudilin Mediated Inhibition of Myosin Motor Activity [Dictyostelium discoideum],4AE3_A Crystal structure of ammosamide 272:myosin-2 motor domain complex [Dictyostelium discoideum AX4]
1MMN_A	1.75e-78	3	763	76	756	X-Ray Structures Of The Mgadp, Mgatpgammas, And Mgamppnp Complexes Of The Dictyostelium Discoideum Myosin Motor Domain [Dictyostelium discoideum]
1MMG_A	1.75e-78	3	763	76	756	X-Ray Structures Of The Mgadp, Mgatpgammas, And Mgamppnp Complexes Of The Dictyostelium Discoideum Myosin Motor Domain [Dictyostelium discoideum]
2JHR_A	2.17e-78	3	770	87	778	Crystal structure of myosin-2 motor domain in complex with ADP- metavanadate and pentabromopseudilin [Dictyostelium discoideum],2JJ9_A Crystal structure of myosin-2 in complex with ADP-metavanadate [Dictyostelium discoideum],3MJX_A Crystal structure of myosin-2 motor domain in complex with ADP-Metavanadate and blebbistatin [Dictyostelium discoideum],6Z2S_A Chain A, Myosin-2 heavy chain [Dictyostelium discoideum],6Z7T_A Nucleotide-free Myosin-II motor domain [Dictyostelium discoideum],6Z7T_B Nucleotide-free Myosin-II motor domain [Dictyostelium discoideum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VNT4|CHS5_CRYNH	0.0	10	1960	8	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	18	1960	10	2002	Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
sp|O13395|CHS6_USTMA	2.16e-285	878	1736	49	900	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VF17|CHS4_CRYNH	4.24e-267	892	1738	154	1000	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	1.12e-139	1243	1727	681	1182	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
1.000058	0.000000

TMHMM  Annotations     

Start	End
903	920
941	963
1210	1232
1600	1622
1632	1654
1661	1683