CAZyme Information: PADG_07913-t30_1-p1

Basic Information

• Species: Paracoccidioides brasiliensis
• Lineage: Ascomycota; Eurotiomycetes; ; NA; Paracoccidioides; Paracoccidioides brasiliensis
• CAZyme ID: PADG_07913-t30_1-p1
• CAZy Family: GT4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1861	KN275969|CGC2	206917.59	7.4481

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PbrasiliensisPb18	8522	502780	132	8390

• Gene Location: location=KN275969:294823-300676(+)

Full Sequence      

MTLNSLTGTIPSHAQSSLPSLPAYLQSDTHLTAHLASRFYVSLPTARLSSQGLICLNTYT
TSTRGPDGQKEGSAMGEADDLARRAWARLGGRGENQAIIFLGESGSGKTTVRSHLLSSFL
ALSSTPLSAKLSLAAFVFDTLTTTKSITTPIASKAGLFFELQYDASSTINPTLIGGKILD
YRLERSRIASVPTGERSFHVLYYLLAGTTAAEKAHLGLDHSIDLRSGGSGNRSSGTISHK
RWRYLGHPTQLKVGINDAEGFQQFKNALRKLQFPRSEIAEICQILACILHIGQLEFTTGQ
ATLTSAEESGGYSHEGGEIVTIVKNKDVLGNVAAFLGLSVAELETSLGYKTKTIHRERVT
VMLDPKGARENADDLARTLYALLVAFVMENINQRICAAEDSVANTVSIIDFPGFAQSAAT
GSTLDQLLNNAATESLYNYCLQSFFDRKAELLETEEVSVPATSYFDNSDAVKCLLKQGNG
LLAILDDQTRRGRTDTQLLEALRKRFENKNPAISVGSATATLPGSNFASKNLAATFTVRH
FAGEVDYPIHGLVEENGDMVSGDLMNLINSTRSSFVRELFGQEALQTVRHPQEKSAIMQA
QVMSKPLRMPSMARRKMDGPARLKALAAQEENDDDDISGSGGSASGSKRQKKGSPVFGPN
QGAAAQFLASLNIINKSLTATNVNPYFVFCLKPNDRRIANQFDSKCVRTQVQTLGIAEIS
QRLRNTDFTVFLPFSEFIGLSDTESVIVGSDKEKCQLVVDERRWPANEARVGSTGVFLSE
RCWADIAGVGERVVPSYSGDGMDDGGDGMLGVGTKMPYGDSKVRLLNSPDLSPGAFIYGD
ETKQGFYSAREIDSRSDAGASAFNSGDMFKNLETREQMAEKGNERKMEEVDDVVVSGSRK
RWLAIVYMLTFYIPDFIIRIIGRMKRKDVRVAWREKFAINLIIWFSCGLAVFFIVVFPRL
LCPKQHVFSPSELSSHDGKGNNQAYIAIRGEVFDLGAYIPSHYPKIVPREALRKYAGMDA
TKLFPVQVSELCKGVDGSIDPSVLLDFTSPNRTGSVTVSRDNDPNAQYHDFRAFTNDSRP
RWYSDKMNMLRMNYRKGYVGYSPRYLKTLADKDQSLAVLDGYVYDLTNYIIGGRRIKAPP
GEDLPENVNVNFMDPLVVDLFQQRPGQDISELFRRLPLGDNESTMRACLTNLFQVGKLDT
RSSIQCQFSQYFVLAVSILLVTIIGFKFFAALQFGRKNLPENLDKFIICQVPAYTEDEES
LRRAIDSMARMRYDDKRKLLVVICDGMIIGQGNDRPTPRIVLDILGVSDTVDPEPLSFES
LGEGMKQHNMGKVYSGLYEVQGHIVPFLVVVKVGKPSEVSRPGNRGKRDSQMLLMRFLNR
VHYNLPMSPLELEIHHQIRNIIGVNPTFYEFILQVDADTVVAQDAATRMVAAFLHDTRVI
GLCGETGLTNAKSSMITMIQVYEYYISHNLTKAFESLFGSVTCLPGCFTMYRIRSVDTGK
PLFVSREVVEAYSEIRVDTLHMKNLLHLGEDRYLTTLLLKHHPKYKTKYIFNAHAWTIAP
DSWAVFMSQRRRWINSTVHNLIELIPLQQLCGFCCFSMRFVVFVDLLSTVIQPVTVAYVV
YLIVLIAVNPSLIPITAFILLGAIYGLQAVIFILRRKWEMVGWMIIYILAMPVFSMGLPL
YSFWHMDDFSWGNTRIVTGEKGRKIVISDEGKFDPASIPKKKWEEYQVELWEAQTQQDDR
SEVSGVSYGTRSYHPAASEYGFPASRPASQIELNRFVTSRMSLAPSDTLGNGPEMEMVDL
MGLPSDDSLLAEIRDILRTADLMTVTKKSIKAELERRFNINLDAKRQYINSATEAVLSGQ
L

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1223	1728	1e-245	0.9924098671726755

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
276845	MYSc_Myo17	0.0	26	786	1	645	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	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).
214580	MYSc	6.67e-155	15	791	11	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	1.23e-80	81	779	60	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	6.59e-71	1248	1580	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
ABV31247.1|GT2	0.0	1	1861	1	1861
QSS67452.1|GT2	0.0	1	1861	1	1866
QSS57527.1|GT2	0.0	1	1861	1	1863
AAR88368.1|GT2	0.0	11	1861	5	1857
AAQ05979.1|GT2	0.0	11	1861	5	1857

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5I0H_A	3.87e-46	81	780	136	728	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	6.35e-46	81	780	134	726	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	9.04e-45	81	780	134	726	Rigor myosin X co-complexed with an actin filament [Homo sapiens]
6C1D_P	3.36e-40	81	778	82	682	High-Resolution Cryo-EM Structures of Actin-bound Myosin States Reveal the Mechanism of Myosin Force Sensing [Rattus norvegicus],6C1G_P High-Resolution Cryo-EM Structures of Actin-bound Myosin States Reveal the Mechanism of Myosin Force Sensing [Rattus norvegicus],6C1H_P High-Resolution Cryo-EM Structures of Actin-bound Myosin States Reveal the Mechanism of Myosin Force Sensing [Rattus norvegicus]
4L79_A	3.82e-40	81	778	87	687	Crystal Structure of nucleotide-free Myosin 1b residues 1-728 with bound Calmodulin [Rattus norvegicus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4P9K9|CHS8_USTMA	0.0	35	1858	25	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	81	1858	101	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	2.58e-281	885	1747	56	912	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VF17|CHS4_CRYNH	2.28e-275	884	1759	148	1037	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	3.87e-133	1248	1745	686	1201	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
1.000054	0.000001

TMHMM  Annotations     

Start	End
902	924
937	956
1208	1230
1606	1628
1632	1654
1661	1683