CAZyme Information: ORE10556.1

Basic Information

• Species: Rhizopus microsporus
• Lineage: Mucoromycota; Mucoromycetes; ; Rhizopodaceae; Rhizopus; Rhizopus microsporus
• CAZyme ID: ORE10556.1
• CAZy Family: GT49
• CAZyme Description: chitin synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1903		216693.46	6.4634

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RmicrosporusATCC52814	11554	N/A	58	11496

• Gene Location: location=KV921864:53403-59285(-)

Full Sequence      

MQDDSRIDLTCLLTSSSPPSEDNITHLLQTRFKRNQPYTRLGHSTLIVVNPYQPLEILND
VTLSTYADIGYRNIVENKPFMQPHVYDLATRVYFHMRRTGEDQSIILSGITGAGKSTTRS
HLLKQLLLLSTHSKKETKLGLQIQNAQIILEAFGHTRTSQNNSASKFGMFQELQFSERGR
ILGAKTLTYAFDKSRVTQVPKDERTYNVFYSLLAGTSVEEQTALHINFPPESFHYLSQSK
VIRQPEDEVAFADLKNALKVCGFKAKTVTQIFQLLSAILHIGNLQFQGDDSSQQTQEACS
IRNYDTLEMVALMLGVSPSKLEQSLTYKLRLIRKELCTMFLNTQGAAEQRDSLARALYHV
LFLWIVEALNTKLCYSSEPANFIGILDQFGFQNFKSNGFEEFCANFANERVHQFIIDQRF
NNQVGINALMTRDGVPLPSIITMDNSACLELLVGKEQDHNISSREKTKSAALGLGGIVGA
MDRDCAKYQTGATDATNANFLANVQRLHSAHPSFSKSQHAYSFGVNHFSGTVHYTVESFL
EKNLDDLSPDFVSLLRDNSTNTFVSTLFESTAMATESHPKDDRTIVKAQLTSKPTRAPSM
KKPKRRDIIPEEDQKAIKDAEDAYQNMQVTTVMDQLYMTLRDLFYTMADTRIYQIIHIRP
NDTLSPDLFDLKRVKAQVRTFLLSDLTARASVEYANYLTFSEFLVRYERLVSSLQIDHVK
SERDQVEDVRAIMNWNESQVFIGHEMIWIAYDTWKELEDGLRAAEKEERERAKEAKQGMM
QDAPVMPSQGYYPESQDRLMPPAAYGDPRGYDEASYVDSEDGIKRDMEGSQWGEESEWGG
VKISDGFGPNMDMSKMVEDYHQPQHESVEEVPITAVRIWWVRFVWLMTFWIPSPFLRWFG
KMKREDVQMAWREKVTLCMLIFFFSAVTIFFIVGLGEVICPGTQHMYSTANVAAHNLPDD
MWVSVRGTVYDITNFARTQHGASGNIATTDLMDQIGGYDMSDSIPPPLTTACQGLVTSST
IKITPNVTTVRASFIHNSGDQNPIPTLTKMSSPTWYWDYFLPTMSLYKKGQLVIPISGLY
SDYQSWSRLALAINGKVYDITDYMSTAKTYDSGSTSSAYHFLHPTVEEIFTKFSGTDATD
KWNQYKASMTSEQQAQNMACLDNYFYIGNVDERDTPRCMFTNYFLVACAGLMGLVILVKF
LAALQFGGAPTPEDHDKFVICQVPCYTEDEESLRKTIDSLTVMNYDDKRKLLFIIADGMI
MGSGNDRPTPRIVLDVLGYDTKNDPEPLMFKSIGEGSKQLNYGKVYSGLYECEGHVVPYI
VIVKVGKASERAKPGNRGKRDSQMICMNFLNKVHFDSEMTPLELEIYHQIKNVIGVNPSF
YEYILMVDSDTEVLPNALNHMISCMLHDGRIIGLCGETKLVNEDRSWTTMIQVYEYYISH
HLAKAFESLFGSVTCLPGCFCMYRIRTPVKNEPLIISPKVIHDYSDNHVDTLHKKNLLHL
GEDRYLTTLMMKHFPQYKMKFTPHAQCKTVAPDRWKVLLSQRRRWINSTIHNLFEVVLLP
DLCGFCCFSMRFVVLIDLIGTLSLPVSVVYLVYLLYVIISKTGPFPMLAIIMLACVYGLQ
ALLFIVKRQWQHIGWMIFYILAIPVFSFFLPIYSFWHFDDFSWGNTRVVVGDKKQKKIIV
ADDEKFDEKMIPLKKWSVYEQELWEMGSTGSKETRLTGHTYKSYQTHGSRNNPSVMYDSR
TQYAGSQAGDYDYYRDTTMHENKRTRSPGYTGSVIAGSEYGGAATHDFMMTPPPMPRQQQ
AMSVHSFGPDYHEMNNTFDVPMRPTSQFSIPLSQGGMLPMLPPGFPSDDEILSEIRNILQ
TANLMSITKKQVREQLSAFFGYDMTPKKEFINTSIEYILKGQL

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1196	1702	2.1e-242	0.9924098671726755

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
276845	MYSc_Myo17	0.0	19	759	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	1196	1702	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).
214580	MYSc	1.22e-149	8	759	10	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.
276950	MYSc	4.19e-148	22	747	1	630	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	1.32e-116	28	707	7	618	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
CDS05327.1|GT2	0.0	1	1827	1	1896
CDS03648.1|GT2	0.0	1	1790	1	1901
CDS05755.1|GT2	0.0	8	1899	6	1832
QDK64620.1|GT2	0.0	8	1899	6	1969
AZQ26804.1|GT2	0.0	8	1899	6	1969

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7KCH_A	1.57e-76	13	725	58	696	Chain A, Unconventional myosin heavy chain [Chara corallina]
5KG8_A	8.36e-75	23	716	76	693	Rigor myosin X co-complexed with an actin filament [Homo sapiens]
5I0H_A	8.69e-75	23	716	78	695	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	2.25e-74	23	716	76	693	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]
3MKD_A	2.59e-71	20	589	97	632	Crystal structure of myosin-2 dictyostelium discoideum motor domain S456Y mutant in complex with adp-orthovanadate [Dictyostelium discoideum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4P9K9|CHS8_USTMA	0.0	5	1899	2	2002	Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
sp|O13395|CHS6_USTMA	0.0	866	1783	59	980	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VNT4|CHS5_CRYNH	0.0	15	1899	17	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|J9VF17|CHS4_CRYNH	2.70e-315	805	1899	85	1268	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	9.30e-153	879	1795	74	1038	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
1.000044	0.000000

TMHMM  Annotations     

Start	End
878	900
917	939
1179	1201
1572	1594
1604	1626
1633	1655