CAZyme Information: FOYG_14032-t42_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOYG_14032-t42_1-p1
• CAZy Family: GH78
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1042		114320.83	5.5461

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FoxysporumNRRL32931	17642	660029	362	17280

• Gene Location: location=JH717847.1:2418874-2422487(-)

Full Sequence      

MAFMAIAILFLCLATFANAENTRQLHGSRARNHRRANVITKAPAWAKEITNSPGHQNPAM
APPDPTVELELSDDSATSLDQYYKDAENATESSDVSPNKSNLSRRSLEKRGSGPLYCKDG
PCADDSCCGPEKICGYGPDYCGKGCSSNCDATAMCGEYSEEGEMPCGMNLCCSASGWCGT
TEVFCDNADPVHKTLPCQAGYGSCNIASSPSCAKGSGSTNGRTIGYYQSWNVRARKCDTK
TPKQLNTKGFTHLFYSFAFIDPVSFKVTPAHDDDVKQMREFTDLSKDGKLQTWIAIGGFD
FSNENTSTHTTWSDMVSTKANRASFIDSVRAYMDEYGFQGVDLDWEYPGEPKRGGRKLAD
TRNFSMLLKEMRAAYGSKYGISLTLAPDYWYLRWFDAKAMEPYVDFFGFMAYDLHGYWDE
DVKTLGKIIRGQADIREIGNNTIPLWFGGLDPKKLNFGLALYGRGYTVADKSCNNLGCSF
VGPSKKGECTDSDGVMSLGEIKNLIKKGVKSTYLKDSMMKQITFDDQWIGYDDEETFADK
KAWADGYCFGGTMIWSIDFQPSDNSTDGSGDVPALPDLDGIGAIPKELQDKVLKKCDTGF
SYDNYGDLPKLWYDSGAEQWADAYIKSQKDHTNWAQNLYRNLFEKKDHTKFSCVTPNSRC
DFDASCAEFNKIGKGGLYYLFQSMSSFHTFMKALNQQFDSKITLTLATVSEMRLILDIKS
GLPQTTINIGSVLGSAFSMASAIAAPIPAVGGPLAGISGLASMIGTFTSTVGGNDNAVDA
TDTLTFAVKTAAVEGKRKIASIVSSVYGDFGHAQADLPKTMLVGGADNPAIKVFGYGAWL
RDNDLTDLSGAVERMSDKMNQALLWQMARLFKGFYVVIRDDLPINKCTHPNNAWDDRTGR
CLDILSWWPKSASGRVGGDLAMEKVWDKWNMSPLWTLRNAVECWENNGGKIGEAKVKALQ
SEWTDGVPPPCFFAMPVLKGNWSKDAASDGAIWLAGDFVGQEGQAGRLWPKDKCDKANRE
LDPITGGQVKKCSSLNKVGGEK

Enzyme Prediction     

No EC number prediction in FOYG_14032-t42_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	221	564	1e-52	0.9493243243243243

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119351	GH18_chitolectin_chitotriosidase	1.12e-64	226	559	4	340	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.
214753	Glyco_18	2.53e-64	222	558	1	332	Glyco_18 domain.
119357	GH18_zymocin_alpha	1.14e-62	222	560	1	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.
395573	Glyco_hydro_18	1.48e-59	222	559	1	306	Glycosyl hydrolases family 18.
119365	GH18_chitinase	7.40e-43	224	558	2	320	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
QKD61159.1|CBM18|GH18	0.0	2	1042	9	1056
QPC60799.1|CBM18|GH18	0.0	2	1039	8	1049
QPC78129.1|CBM18|GH18	0.0	2	1039	9	1053
CZS83249.1|CBM18|GH18	0.0	2	1039	9	1065
CEF88836.1|CBM18|GH18	0.0	2	1039	9	1065

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1LG1_A	3.52e-38	222	578	2	360	Crystal Structure Of Human Chitotriosidase In Complex With Chitobiose [Homo sapiens],1LG2_A Crystal Structure Of Human Chitotriosidase In Complex With Ethylene Glycol [Homo sapiens],1LQ0_A Crystal Structure Of Human Chitotriosidase At 2.2 Angstrom Resolution [Homo sapiens],6ZE8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_B Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_C Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_D Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_E Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_F Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens]
1GUV_A	3.60e-38	222	578	2	360	Structure of human chitotriosidase [Homo sapiens]
4WJX_A	4.57e-38	222	578	2	360	Crystal structure of human chitotriosidase-1 catalytic domain at 1.0 A resolution [Homo sapiens],4WK9_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (0.3mM) at 1.10 A resolution [Homo sapiens],4WKA_A Crystal structure of human chitotriosidase-1 catalytic domain at 0.95 A resolution [Homo sapiens],4WKF_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (2.5mM) at 1.10 A resolution [Homo sapiens],4WKH_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (1mM) at 1.05 A resolution [Homo sapiens],5NR8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7a [Homo sapiens],5NRA_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7g [Homo sapiens],5NRF_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7i [Homo sapiens]
6JJR_A	4.98e-38	222	578	2	360	Crystal structure of human chitotriosidase-1 (hChit1) catalytic domain in complex with compound 2-8-14 [Homo sapiens],6JK6_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 2-8-s2 [Homo sapiens]
1HKK_A	6.32e-38	222	578	2	360	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q13231|CHIT1_HUMAN	1.30e-36	222	578	23	381	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q6RY07|CHIA_RAT	6.46e-36	224	585	25	390	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q91XA9|CHIA_MOUSE	8.70e-36	224	587	25	392	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|P09805|KTXA_KLULA	8.94e-34	153	571	317	726	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|Q9D7Q1|CHIT1_MOUSE	1.27e-32	222	587	23	388	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000251	0.999710	CS pos: 19-20. Pr: 0.9785

TMHMM  Annotations     

There is no transmembrane helices in FOYG_14032-t42_1-p1.