CAZyme Information: RO3G_04443-t26_1-p1

Basic Information

• Species: Rhizopus delemar
• Lineage: Mucoromycota; Mucoromycetes; ; Rhizopodaceae; Rhizopus; Rhizopus delemar
• CAZyme ID: RO3G_04443-t26_1-p1
• CAZy Family: GH134
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1640		184614.87	6.0595

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=CH476734:601565-606690(-)

Full Sequence      

MVGSKTLHYSLESSRVTGDCVPASLDGNFNIFYYLLAGVSPEEKATLQLMDASSYPYLQK
FSKRSISSVDAQHFEELKLAMKTCGFRKEQIGRIIQLVATILHLGNLSFVDPAGTGTQEA
AFVKNTELLDLVADFLGLDPHALENVLTFKTTMIRKDVTTLILNAEQAAHQRDELCQVLY
SLLFSWIVEKINSKTCIEDFTSFIGVLDFPGLQSYYSVAGFEQLAINLANERIQEYIDHT
MFRLEADQYRAEGVHVPDVNPQSSALDLLTRPKGICHEINTMTDVSKRAYTDNNIMDSII
KYNTTHSAFSVKNSDTSARHFVIQHYGNTPVEYSTQGFIEQNNSQISVDFLSLFKGGMDV
QPSWNSFIVELFANVKTQSHPKHNTAIISAQQSAKPMRGPSQRRSTRRKGGSNEKGGNTT
DNSTSATSTVLSQIQSALDELIASFEEAKLWVVYCILPKYKETGSVDTKLVQSQIDSFRI
PSLLQLPAVSYVESYNHQDFLDRYGHLFQELDTSRLLRSQCEMAAGIMNWTTPDMSITQN
KVFLSAVAWRELEDQLRSYEKIEQRQARDHGREDETSVSHPFSGAAAAAAAAGLPLPPQN
HYDNDTGSFYSEDESGQYMENEGSLYGSESYFSQQGGLALVPQQEPVVENLDETEEDEAR
MTPARKRWLYFVTFCTWWIPSKFLIWCGRMKRKDVRVAWREKVTLCMLIFLLCAFIIWFL
VFFSEAICPKENVYSTSELANHGKDNTKGAYVAIRGEVFHLTNFAPHHYPQTLVPTSSVM
EYAGSDATDLFPVQVSALCEGVSPYVSLDYTVNLTDSNAQYHDFRYTSDAYNPNWYYDQM
TLLRKNYKVGNMGYDWKSISDQAKSATTINGIKALRIWAVIDKRVYDLTTYTMGGRYAKG
PGNAAAPSGIDTNFLNPQVVELFQQQSVVTILLAAVIVFKFIAALRFGGRRAPEEHDKFV
ICQVTCYTEDEGSLRKTIDSIARLDYDDKRKLLFVICDGMIIGSGNDKPTPRIVLDILGV
DPQVDPEPLSFVSVGEGAKQHNMAKIYSGLYEVAGHVVPYIVVAKCGNPRERQKPGNRGK
RDSQLVLMQFLNRVHYDAPMNPMQLEVYHQMKNVIGVSPHFYEFVLMVDADTEVMPDGLN
FLVASAVHDSKIIGICGETNLSNEKDTWVTMIQVYEYFISHHLIKSFESLFSTVSCLPGC
FTMYRVRTVDGKRALFISNEVIADYSVNIVDTLHKKNLLHLGEDRYLTTLLLKHFADFKT
KFTPDAKCQTNAPDLWSVLVSQRRRWINSTVHNLGELIFLPRLCGFCCFSMRFIVMLDLI
STLAMPALLGYLGYLIYTLATLDGDTVPIITIATIAGTYGLQALLFIVKGRWEFIMWMLV
SILAMPVFSFYIPVYAYWHFDDFSWGNTRVVVGEKGKKVAVVADEGTFDPKSIPTMKWSD
YEQQLLSEDQWSDNISHSSGYTHGSRGYPHTGSESVYGAPSGMMMMPDNMSVYSAARSQQ
QRQSMGFDHNSMVFPSNNSMPMMPYGNGSSQMLPSSRSMASFAPAQQLNSPGQYIPLQTS
SQFNKAPSSHSLLMDGFEQGDGIKNEEIMIQVQRILETADLTKVTKKQVREELQNYFGVS
MQSRKDYINACIENVITNHV

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	936	1443	5.4e-229	0.9924098671726755

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
367353	Chitin_synth_2	0.0	937	1444	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).
276845	MYSc_Myo17	8.60e-139	1	554	163	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.
214580	MYSc	3.80e-88	1	557	171	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	1.11e-83	1	545	158	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	2.75e-74	961	1293	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
CDS06114.1|GT2	0.0	1	1640	180	1895
CDS06732.1|GT2	0.0	1	1636	188	1883
CDS08031.1|GT2	0.0	1	1446	179	1690
AZQ26801.1|GT2	0.0	3	1636	189	1906
QDK64613.1|GT2	0.0	3	1636	189	1906

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5I0H_A	2.33e-48	3	553	237	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	3.96e-48	3	553	235	733	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]
5KG8_A	9.70e-48	3	553	235	733	Rigor myosin X co-complexed with an actin filament [Homo sapiens]
7B1A_A	5.11e-47	3	504	266	716	Chain A, Myosin-2 heavy chain [Dictyostelium discoideum]
2Y0R_X	9.00e-47	3	504	254	704	Structural basis for the allosteric interference of myosin function by mutants G680A and G680V of Dictyostelium myosin-2 [Dictyostelium discoideum],2Y8I_X Structural basis for the allosteric interference of myosin function by mutants G680A and G680V of Dictyostelium myosin-2 [Dictyostelium discoideum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4P9K9|CHS8_USTMA	0.0	1	1637	182	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	3	1637	198	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	1.97e-265	657	1479	62	932	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VF17|CHS4_CRYNH	6.09e-246	662	1442	160	989	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	4.55e-142	961	1443	686	1183	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
1.000048	0.000001

TMHMM  Annotations     

Start	End
668	690
703	722
927	949
1319	1341
1346	1368
1375	1397