CAZyme Information: HMPREF1544_02845-t46_1-p1

Basic Information

• Species: Mucor circinelloides
• Lineage: Mucoromycota; Mucoromycetes; ; Mucoraceae; Mucor; Mucor circinelloides
• CAZyme ID: HMPREF1544_02845-t46_1-p1
• CAZy Family: CE9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1904		215448.40	6.5382

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Mcircinelloides1006PhL	12410	1220926	183	12227

• Gene Location: location=KE123922:103660-109570(+)

Full Sequence      

MTQQQQPLSVSDLTQLTRDPSSDELAELLRQRYLNDVIYTNISPSILIAVNPYHPNSTVK
ADYIAEYKDTSSAKANQWKEPHIYQLVNHAYLHMRRTSINQSILFSGESGSGKSEQFRQS
INHLIALSTHRKTTRTQANVIHAQIILRAFSHAKTTQHDNASRSALFAEIHFSERGRLAG
AVFLPYALEKQRVSAAGQDERNFHVFYNLLAGATVEEKTRLGLSDWSTFQYLSKTSTSRA
SSLDDASADAELRIALKTVLFQKHRVAQVYQILAAILHLGNIHFIEDANNSQDAAIIKNI
DTLTTAADLLGVDPNALMSSLTFKSKLIKRDITTLFLDPEQASKQRDDLAQSLYCLLFTW
LVEQINDRLAPKSSHSFIGLLDLPGWVYSRPSGAGFDQLAFHFIQETVHQFMYVNIFDRD
RQEYADQGLTISNDQWPTSPAVVDLFVHPSKGLWSIMNAQASRQQNQHRYDDGETLMDNY
ASANKSAINEQLLAFKKSDTDSKLFSIQHFWGSTTYEPRSFTERNQDYLCNDFIALFSGN
AYNPPTSNSLVACLFDDNILGHDDGTRNRVFSQQQGIRPLRSPTATTTTTTYTHTAISSS
VNDHKAEVKSTLSTSLQSDVLTIADLLVTGVSDLTQALSYTLPWSVLCIRPNDLSLPNSC
DVKKVAVQQSHFKLLDMIRRMKSGYYTTVFTLEEFWDRYHVSLPLTMNTMLDMNLPLKER
CVYMAQSLGWNETWVAVGKSKIFLSNNAFRILEDDLRSLEKTESKKAKMSLMGGSLPGQK
PFDMYSFNDDVMSSAVSEDDYMDEAGLHEFNGSEVFSQATFDNKRSNTLLMSGSTQQDYA
GMNEKEDLKAADASPPEEEDEPTTGIRRKWLMFVWFLTWWVPSPALNHCGGMKRRDVRLA
WREKVALCLLIFLLSAAMVIFIVFFGPLICPHQDVYSLSELQGKTDKDSAYVAIRGEVFD
LTKFAPHHWASEVIPDNVIFDYAGKDATNLFPVQVSALCDGTTGRIPEELVLDFQVNLTD
RNAAYHDFRFFTNDYRPDWYFEQMVYMRKNYRLGFMGYEPADILRQATNVVNVGDISTHR
SWATLHGDVYDLTYYLMGGRAPRAPEGMTPPANLDLNFMDNSIVQLFRQLAGTDISKHFD
ALPISEDLRMRQLVCLRNLFFVGKLDTRRSLQCQFSEYFLLIVTGFLCAVILFKFLAALQ
LSSFREPEDYDKFIVCQVPCYTESEESLRKTIDSIAVLRYDDKRKLLFLVCDGMIIGSGN
DRPTPRIVLDILGVDPNVDPEPLSFLSLGDGIKQHNTAKIYSGLYECSGHVVPYVVVVKV
GAPNERQKPGNRGKRDSQMVLMRFLNKVHFESLMTPMELEIYHQIKNVIGVNPSFYEFVL
MVDADTEVLPDSLNRMVSCFVHDSKVVGLCGETKLANEKDSWVTMIQVYEYYISHFLSKA
FESLFGSVTCLPGCFCMYRIRSPGKNQPLLVSNQVIVDYAENKVNTLHQKNLLHLGEDRY
LTTLILKHFPTYKTKFTADAGCLTNAPDRWSVLLSQRRRWINSTIHNLGELVFLPQLCGF
CCFSMRFVVILDLLSTLVMPAVVCYLGFLIYRLATNAGQVPFISIITLCGVYGLQAIIFI
VRRKWEHIGWMIVYILAIPLFSFFIPMYSFWHFDDFSWGNTRLVLGDDGQKKVLPADEGK
FDPKSIPLKKWSDHENELWETGSAETRGTTITSSTTRRTASGLPPVVGYSPTNNGFMTPV
VNYASSMNQIPMAPTAAGSVINGGQVYNDNASFRYSHQNLAGRASSVIMGPPSVLNMAPM
QQQQQAPHQMNMMSAPSIYSEASATHGGIMYPSIMNNSGMLDNSNVYHPTDEEIRREVQR
ITATADLMTMTKKQVREQLSRHFGINMSYRKDFINFCIEEALNY

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1189	1697	3.6e-239	0.9962049335863378

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
276845	MYSc_Myo17	0.0	20	754	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.
367353	Chitin_synth_2	0.0	1188	1697	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).
276950	MYSc	2.00e-131	29	745	7	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	6.73e-126	9	754	7	674	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	1.73e-109	29	744	7	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
CDS08031.1|GT2	0.0	10	1698	11	1689
CDS06114.1|GT2	0.0	21	1902	21	1891
CDS03322.1|GT2	0.0	128	1902	5	1618
CDS06732.1|GT2	0.0	9	1902	12	1883
AZQ26801.1|GT2	0.0	1	1902	1	1906

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KG8_A	7.13e-66	10	753	63	733	Rigor myosin X co-complexed with an actin filament [Homo sapiens]
5I0H_A	9.94e-66	10	753	65	735	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	1.70e-65	10	769	63	745	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]
7RB9_D	1.28e-64	10	753	4	675	Chain D, Isoform 3 of Unconventional myosin-XV [Mus musculus]
3MYH_X	1.52e-64	29	557	106	614	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|Q4P9K9|CHS8_USTMA	0.0	10	1903	7	2003	Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
sp|J9VNT4|CHS5_CRYNH	0.0	1	1902	1	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	2.84e-305	841	1700	46	896	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VF17|CHS4_CRYNH	1.12e-276	863	1751	159	1039	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	1.36e-143	1215	1697	686	1184	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
1.000042	0.000000

TMHMM  Annotations     

Start	End
870	892
905	927
1175	1197
1567	1589
1599	1621
1628	1650