CAZyme Information: KAF5669574.1

Basic Information

• Species: Fusarium circinatum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium circinatum
• CAZyme ID: KAF5669574.1
• CAZy Family: GH1
• CAZyme Description: glycoside hydrolase family 18

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
421		47051.76	5.9256

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FcircinatumNRRL25331	13905	N/A	0	13905

• Gene Location: location=JAAQPE010000321:4174-5691(+)

Full Sequence      

MMWIHKTLPCQAAYGSCNIASSPSCARGGGSTNGRTIGYYQSWNVRTRKYDTKTPNQLDT
TGFTHLFYSFAFIDPVSFNVPPAHDDDVKQMREFTDLSNNGTLQTWIAIGGFDFSNENTS
THTTWSDMVSTKANQAAFIQSAGAYMDAHGFQGIDLDWEYPGEPERGGRKLADTRNFSML
LKEMRAAYGSKYSISLTLAPDYWYLRCFDAKAMEPYVDFFGFMAYDLHGYWDEDVKTLGK
IIRGQADIREIGNNTIPLWFDGLDPKKINFGLALYGRGYTVADKSCNSLGCSFVGPSKKG
ECTDSDGVMSLGEIKNLINKGVNSTCLRDSMMKQITFDEQWIGYDDEETFADKKAWADGY
CFGGTMIWSIDFQPGNNSSVSALPSTLPSTLVNVSVETFISKSNKHTGKPYRNQKLVRLN
Q

Enzyme Prediction     

No EC number prediction in KAF5669574.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	34	380	4.4e-53	0.9594594594594594

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119351	GH18_chitolectin_chitotriosidase	9.74e-67	39	372	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	3.12e-65	35	371	1	332	Glyco_18 domain.
119357	GH18_zymocin_alpha	8.54e-61	35	373	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	1.53e-57	35	372	1	306	Glycosyl hydrolases family 18.
119365	GH18_chitinase	1.00e-43	37	371	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	2.32e-254	4	380	198	574
QPC60799.1|CBM18|GH18	4.31e-243	4	381	187	565
CZS83249.1|CBM18|GH18	4.94e-243	4	379	199	575
CEF88836.1|CBM18|GH18	4.94e-243	4	379	199	575
QPC78129.1|CBM18|GH18	1.95e-242	4	381	188	566

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1GUV_A	1.80e-37	35	373	2	342	Structure of human chitotriosidase [Homo sapiens]
1LG1_A	3.40e-37	35	373	2	342	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]
4WJX_A	4.31e-37	35	373	2	342	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	4.65e-37	35	373	2	342	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	6.42e-37	35	373	2	342	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	9.99e-36	35	373	23	363	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q6RY07|CHIA_RAT	3.73e-34	39	391	27	383	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|H2A0L4|CHI1_PINMG	4.81e-34	39	373	27	358	Putative chitinase 1 OS=Margaritifera margaritifera OX=102329 PE=1 SV=1
sp|P30922|CH3L1_BOVIN	6.31e-34	35	373	23	357	Chitinase-3-like protein 1 OS=Bos taurus OX=9913 GN=CHI3L1 PE=1 SV=3
sp|Q29411|CH3L1_PIG	1.21e-33	35	373	23	357	Chitinase-3-like protein 1 OS=Sus scrofa OX=9823 GN=CHI3L1 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.998666	0.001357

TMHMM  Annotations     

There is no transmembrane helices in KAF5669574.1.