CAZyme Information: FOXG_10827-t26_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOXG_10827-t26_1-p1
• CAZy Family: GH2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1085		118892.14	7.0745

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Foxysporum4287	21354	426428	429	20925

• Gene Location: location=CM000589.1:3760-8264(+)

Full Sequence      

MSQIKIFLLFASPGLLLSLSLSLVQAQVSVANGVSVYQGTTVSQNQHGIPTLAYNCAKVP
ASCENVHQQYPLATTVHAAPAGAVTGHHTILGARSHLQLHFDRNDNIGGQRGKACAKSWK
NHHNCPESNQPDTVPSGAMLGDDSFPAARWNPNNLVMGDAGYNRIANAAGQFSGNSTNPA
RQAYKDLPKGPPLPILEIAQDFVEEQKEDKPAEEPYIVRAVKASDGNESSIVEIEDSKAL
TPRAADTSGWMHRRQSKRQCDFVTPCPDGSCCNRKRQCGYGEEVCGSKVCVSNCDATAAC
GKDSLGGKVKCPLNVCCSAYGYCGVEDDFCRAGNADNSCQKGFGSCTKIEPPSCGGRSAF
ARSIGYYQFANVRERQCNRITPKQIRTEGFTHFLARRARFIKSLTSFLDENGFQGVELDW
EYPGAPDRGGRKEDTDNYVSLLKDMRAAFGSKYGISIAIHTSYWYLRWFKSKEIEQYVDY
MGIMTYDLHGPWDHDVKQVGRVILGHTNIPEIANWSLPLYYAGVDPAKVNMGLAYYARGY
TVADSNCNGVGCKWSGTSRPAPCTNFGGVMSLEEIERMVKDEPGISPKLLPKDMMMELKF
GNQWIGYDNKDTIYMKKKWASSRCFGGTMVWSVDMFSGSGSGDTPDDQSDGGSEDPGGGQ
GDGSGVIYIDPEIWEVDQPEVKCHPPCTMVLPPSSLKKPVTLTLPPYETSLDVAWSGKDG
WHSTVQKTTLTPLVVTVTTVDVWHITIREDRTKLTTIWSTFDITPSIKVPTFIITNRLPE
TTKDSVTQPPGTKTITPPPYPWTYTPPTTRPSNTPGDDDDDDDEVIPPFPVVTWRPGSLV
LYARRTAASHGGGDFADPRNPKPPKRPVPPNPTIPKPTGKPVKPTKIPTPGTTPENKEHE
DNERQCAIEFGLPLPTWRDPATTTSVKPKPTPPKPSPKPDPKPPSPNPKTEEVKCYGIGG
AWIHRALVIEALEDFCDRYEGQVLDAAKPETERTLECQHGVVCTGDGFGCVVNVLMSVTV
KNGCRFTVGGKGPKSECGRILRRMIDECDASDVRYKKGGTMSSNCADWKFDPNYRGWWSK
NQCSA

Enzyme Prediction     

No EC number prediction in FOXG_10827-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	395	635	3.7e-43	0.6824324324324325

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	1.29e-55	388	635	80	333	Glyco_18 domain.
119357	GH18_zymocin_alpha	1.13e-54	395	636	90	345	Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.
119351	GH18_chitolectin_chitotriosidase	3.99e-50	395	638	95	345	This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.
395573	Glyco_hydro_18	3.02e-46	395	635	87	306	Glycosyl hydrolases family 18.
119365	GH18_chitinase	3.30e-40	395	635	108	321	The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD48531.1|GH18	0.0	3	1085	45	1389
CEI63226.1|CBM18|GH18	0.0	7	1076	2	1222
CDP30264.1|CBM18|GH18	2.61e-120	266	713	120	615
CAP65874.1|CBM18|GH18	2.61e-120	266	713	120	615
CEI60137.1|CBM18|GH18	3.38e-119	226	795	36	640

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HJV_A	3.39e-24	397	639	95	341	Crystal structure of hcgp-39 in complex with chitin tetramer [Homo sapiens],1HJV_B Crystal structure of hcgp-39 in complex with chitin tetramer [Homo sapiens],1HJV_C Crystal structure of hcgp-39 in complex with chitin tetramer [Homo sapiens],1HJV_D Crystal structure of hcgp-39 in complex with chitin tetramer [Homo sapiens],1HJW_A Crystal structure of hcgp-39 in complex with chitin octamer [Homo sapiens],1HJW_B Crystal structure of hcgp-39 in complex with chitin octamer [Homo sapiens],1HJX_A Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes [Homo sapiens],1HJX_B Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes [Homo sapiens],1HJX_C Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes [Homo sapiens],1HJX_D Ligand-induced signalling and conformational change of the 39 kD glycoprotein from human articular chondrocytes [Homo sapiens],1NWR_A Crystal structure of human cartilage gp39 (HC-gp39) [Homo sapiens],1NWR_B Crystal structure of human cartilage gp39 (HC-gp39) [Homo sapiens],1NWR_C Crystal structure of human cartilage gp39 (HC-gp39) [Homo sapiens],1NWR_D Crystal structure of human cartilage gp39 (HC-gp39) [Homo sapiens],1NWS_A Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitobiose [Homo sapiens],1NWS_B Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitobiose [Homo sapiens],1NWS_C Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitobiose [Homo sapiens],1NWS_D Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitobiose [Homo sapiens],1NWT_A Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitopentaose [Homo sapiens],1NWT_B Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitopentaose [Homo sapiens],1NWT_C Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitopentaose [Homo sapiens],1NWT_D Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitopentaose [Homo sapiens],1NWU_A Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitotetraose [Homo sapiens],1NWU_B Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitotetraose [Homo sapiens],1NWU_C Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitotetraose [Homo sapiens],1NWU_D Crystal structure of human cartilage gp39 (HC-gp39) in complex with chitotetraose [Homo sapiens],7CJ2_A Chain A, Chitinase 3-like 1 (Cartilage glycoprotein-39), isoform CRA_a [Homo sapiens],7CJ2_B Chain B, Chitinase 3-like 1 (Cartilage glycoprotein-39), isoform CRA_a [Homo sapiens]
3WL1_A	5.56e-24	397	635	106	358	Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with reaction products (GlcNAc)2,3 [Ostrinia furnacalis],3WQV_A Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with a(GlcN)5 [Ostrinia furnacalis],3WQW_A Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain in complex with a(GlcN)6 [Ostrinia furnacalis]
3FXY_A	7.47e-24	397	635	95	343	Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_B Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_C Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FXY_D Acidic Mammalian Chinase, Catalytic Domain [Homo sapiens],3FY1_A The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3FY1_B The Acidic Mammalian Chitinase catalytic domain in complex with methylallosamidin [Homo sapiens],3RM4_A AMCase in complex with Compound 1 [Homo sapiens],3RM4_B AMCase in complex with Compound 1 [Homo sapiens],3RM8_A AMCase in complex with Compound 2 [Homo sapiens],3RM8_B AMCase in complex with Compound 2 [Homo sapiens],3RM9_A AMCase in complex with Compound 3 [Homo sapiens],3RM9_B AMCase in complex with Compound 3 [Homo sapiens],3RME_A AMCase in complex with Compound 5 [Homo sapiens],3RME_B AMCase in complex with Compound 5 [Homo sapiens]
1E9L_A	7.76e-24	397	639	95	349	The crystal structure of novel mammalian lectin Ym1 suggests a saccharide binding site [Mus musculus],1VF8_A The Crystal Structure of Ym1 at 1.31 A Resolution [Mus musculus]
2YBT_A	8.23e-24	397	635	99	347	Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_B Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_C Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_D Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_E Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_F Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBU_A Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_B Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_C Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_D Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_E Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_F Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	1.11e-29	280	636	287	712	Killer toxin subunits alpha/beta OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 PE=1 SV=1
sp|P36362|CHIT_MANSE	8.15e-26	390	635	112	374	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
sp|Q6RY07|CHIA_RAT	1.61e-25	397	639	116	370	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q95M17|CHIA_BOVIN	3.81e-25	387	635	103	364	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q9W5U2|CHI10_DROME	3.37e-24	397	635	2006	2252	Probable chitinase 10 OS=Drosophila melanogaster OX=7227 GN=Cht10 PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000221	0.999742	CS pos: 26-27. Pr: 0.9754

TMHMM  Annotations     

There is no transmembrane helices in FOXG_10827-t26_1-p1.