CAZyme Information: FOZG_17475-t36_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOZG_17475-t36_1-p1
• CAZy Family: GT34
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
391		42979.21	6.8346

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FoxysporumFo47	18556	660027	365	18191

• Gene Location: location=KI981472.1:18984-20326(-)

Full Sequence      

MHAAPNLVTVALVQIFVARIALLGVMRRVSAILVALAPSLPTIPSALSTSALPSMATVAL
PRISAERKLSIAYLALPRVLCTDPSDIPDGVYTHINFAFASIDPKTFQIIPASSKDPQLY
RELARKKKIDPNLKIFIAIGGWAFNDPGPTITTFSDIARSDANTRTFIKSLISFISTYDF
DGVDIDWEYPAADDREGREEDFDNLPKFLSKIKSALKQSGGRSGLSIAIPASYWYLQHFD
LEKISKYVDHFNVMTYDLHGAWDTPKSWLGNHLNSHTNLTEIKDAFDLLWRNNIDPDQVN
MGLAFYARTFTASSTGCMSTGCLFDAGGPAEPCTNAVGVMSNPEIMRKLGGKIGSGDLDK
TAAIKTVKIGSTWLTYDDVDTWKLKLDFARS

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	86	390	3.4e-57	0.8141891891891891

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	6.14e-76	82	391	16	320	Glyco_18 domain.
119357	GH18_zymocin_alpha	1.21e-69	83	382	19	313	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	4.69e-67	92	391	23	293	Glycosyl hydrolases family 18.
119351	GH18_chitolectin_chitotriosidase	1.29e-66	83	391	19	327	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.
119365	GH18_chitinase	6.65e-60	86	311	20	267	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
QKD46405.1|CBM18|GH18	5.79e-202	84	381	133	430
QGI85804.1|CBM18|GH18	3.84e-201	84	391	178	485
QGI99493.1|CBM18|GH18	2.16e-200	84	391	178	485
QGI68603.1|CBM18|GH18	2.16e-200	84	391	178	485
CCT72994.1|CBM18|GH18	2.16e-200	84	391	178	485

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WUS_A	2.33e-34	84	390	23	327	Crystal structure of a insect group III chitinase (CAD2) from Ostrinia furnacalis [Ostrinia furnacalis],5WVH_A Crystal structure of an insect group III chitinase complex with (GlcNAc)6 (CAD2-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]
6JM7_A	2.95e-33	83	391	24	336	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
5WVF_A	3.02e-33	84	390	23	327	Crystal structure of a mutant insect group III chitinase (CAD2-E647L) from Ostrinia furnacalis [Ostrinia furnacalis],5WVG_A Crystal structure of a mutant insect group III chitinase complex with (GlcNAc)5 (CAD1-E647L-(GlcNAc)5) from Ostrinia furnacalis [Ostrinia furnacalis]
1HKK_A	1.26e-32	84	390	22	327	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1LG1_A	1.28e-32	84	390	22	327	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	2.28e-42	80	346	396	653	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|Q13231|CHIT1_HUMAN	2.96e-31	84	390	43	348	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q6RY07|CHIA_RAT	7.60e-30	84	390	43	350	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|P36362|CHIT_MANSE	3.34e-28	86	390	46	360	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
sp|Q9D7Q1|CHIT1_MOUSE	5.64e-28	84	390	43	346	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.921584	0.078422

TMHMM  Annotations     

Start	End
7	26