CAZyme Information: RO3G_13033-t26_1-p1

Basic Information

• Species: Rhizopus delemar
• Lineage: Mucoromycota; Mucoromycetes; ; Rhizopodaceae; Rhizopus; Rhizopus delemar
• CAZyme ID: RO3G_13033-t26_1-p1
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1442		163163.17	5.8563

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RdelemarRA99-880	17703	246409	244	17459

• Gene Location: location=CH476742:926036-930545(+)

Full Sequence      

MQPHVYDLATRVYFHMRRTGEDQSIVLSGITGSGKSTTRTHLINQLLLLSTHSKKETKLG
SQIKNAQIILEAFGHSKTSQNNSASKFGVFQELQFSERGRILGVKTLTYAFDKSRVTQVP
KDERTFNVFYSLLAGTSLEEQTALHINFPLESFHYLSQSKTIRQPEDEIAFADLKSAFKA
CGFKAKTVTQIFQLLSAILHIGNIQFQNDNDALQQEACNVRNRDALEVVALMLGVSPSKL
EQALTYKLRLIRKELCTMFLNTQGAVEQRDALARALYHVLFLWIVEHFNNKLCYSSDPAN
FIGLLDQFGFQNFKSNGFEEFCVNFANERVHQFIIDQRFNQQVGLNALMSRDGIVLPSIT
TLDNSACLELLVGNEQDHNTTTREKSKSSAALGLNGIVGVMDRDCAKYQTGATDATNANF
LANVQRSHGTHPSFAKSQHAYSFGINHFSGTVHYTVDSFLEKNLDDLSPDFVSLLRDNST
NNFVSALFESTAMATESHPKDDRTIVKAQLTSKPTRAPSMKKPSKRRENVITEDEDASKQ
KAIKDAEDAYQNMQVTTVMDQIYMTLRDLFYSMADTRIYQIIHIRPNDTQAPDMFDLKRV
KAQIRAFLLPDLTARAAVEYANYLTFSEFLVRYERLVSSLQIDHTKPERDQVQDVRAIMN
WNESQAFVGHEMVWITFDTWKELEDGLRAAEKELRERAKEAKQETMQDAPILSGPGYHPD
SHDMLLPRMSYADPRGYEDGASYADSEDGLKRDMEGSQWGEESEWGGMKISDGFGPNMDM
SKMVEDYHQPQYESVEEVPITRLRIWWVRFVWLMTWWVPSPFLRWFGKMKREDVQMAWRE
KLTLCLLILLFSGITIFIIVGLGEVMCPGTKYMYSTANVQAHNVADDMYMSVRGVVYDVT
SFAKTKHGTTGYTATQDLMEQVAGLDVSASIPPPLTQACAGLVTSATVKITPNVSTTMAS
FVHYSGDQTTLTSSSKLTDGRWYWDYFLPTMSLYKKGTLVIPISQLAADYNSWTRLALAI
DGKVYDITDYMSTAQTYSTGTTSSDYHFLDSTVEEIFTKFSGTDATDKWNQYKSAMTAEK
QAQNMNCLNNYFYVGDVDERDSARCMFTNYFLLALAALMGLVTVVKFLSALQFGGAPTPE
DHDKFVICQVPCYTEDEESLKKTIDSLTVLNYDDKRKLLFIIADGMIMGSGNDRPTPRIV
LDVLGYDTKNDPEPLMFKSIGEGSKQLNYGKVYSGLYECEGHVVPYIVVAKVGKASERAK
PGNRGKRDSQLICMNFLNKVHFDSEMTPLELEMYHQIKNVIGVNPSFYEYVLMIDSDTEV
LPDALNHMISCMLHDGRIIGLCGETKVVNENDSWTTMIQVYEYYISHHLAKAFESLFGSV
TCLPGCFCMYRIRTPVKNEPLIISPKIIHDYSDNHVDTLHKKNLLHLGEDRYLTTADDET
LS

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1124	1435	1.7e-145	0.6223908918406073

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
276845	MYSc_Myo17	0.0	2	685	64	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	1.03e-169	1126	1435	7	333	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	5.58e-139	1	685	71	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	1.16e-138	3	673	55	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	3.82e-112	1	675	52	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
CDS05327.1|GT2	0.0	1	1435	83	1517
CDS03648.1|GT2	0.0	1	1435	82	1544
CDS05755.1|GT2	0.0	1	1435	81	1501
CDZ98697.1|GT2	0.0	1	1435	94	1552
QDK64620.1|GT2	0.0	1	1435	86	1539

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3MKD_A	7.15e-68	3	509	152	632	Crystal structure of myosin-2 dictyostelium discoideum motor domain S456Y mutant in complex with adp-orthovanadate [Dictyostelium discoideum]
5I0H_A	7.16e-68	1	642	129	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]
1MMD_A	7.64e-68	3	509	153	633	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]
1LVK_A	1.03e-67	3	509	153	633	X-Ray Crystal Structure Of The Mg (Dot) 2'(3')-O-(N- Methylanthraniloyl) Nucleotide Bound To Dictyostelium Discoideum Myosin Motor Domain [Dictyostelium discoideum]
1MMN_A	1.39e-67	3	509	153	633	X-Ray Structures Of The Mgadp, Mgatpgammas, And Mgamppnp Complexes Of The Dictyostelium Discoideum Myosin Motor Domain [Dictyostelium discoideum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VNT4|CHS5_CRYNH	1.72e-316	2	1435	95	1544	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	2.94e-316	1	1435	80	1556	Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
sp|O13395|CHS6_USTMA	1.21e-223	785	1435	51	698	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VF17|CHS4_CRYNH	3.98e-223	736	1435	95	797	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	1.47e-94	806	1435	74	760	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
1.000031	0.000023

TMHMM  Annotations     

Start	End
805	827
844	866