CAZyme Information: FPRN_13180-t42_1-p1

Basic Information

• Species: Fusarium proliferatum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum
• CAZyme ID: FPRN_13180-t42_1-p1
• CAZy Family: GH76
• CAZyme Description: related to chitinase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1170		129697.83	5.9078

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FproliferatumNRRL62905	15602	N/A	348	15254

• Gene Location: location=FCQG01000026:464472-468098(+)

Full Sequence      

MRLTWATTLVALLLTSTPFTVAEDTHCDKNKPCEVGCCGTNNVCGTGPDYCSKAKCINSC
TYKAECNPGKWDSQYFNATKCPLNVCCSKFGFCGTTEEFCGKETVKRPSCNIGSQSVKRV
IGYYGSGGATRKCNPMIPDAFPQGIYTHIYFAFGSIDPKSFKVVPANAGDQQLYSQLSSL
KTRDSGQELWLSIGGWAFSDKGSPTATTFSDLVNADETRQNVFFASLTLFMQTWGFTGID
IDWEYPVDKDRSGRESDFKAYPRFLKRLKSALDDYKYGLSVTLPTSYWYLQHFDLENIEP
SVDWFNVMSYDLHGAWDIGNKWTGAFVGAHTNLTEITSSLDLLWRNKVSPSKVVLGLAFY
GRSVTLASPSCSEPGCPYLSAGDAGCSGEAGILFNSEISDLIHEKKLRPKLYKDAAIKTI
QWNNDQWVSYDDRDTWKLKANFLKSQCLSGVLVWAVDYDDDKHSYSNGLAAALGIKVNVD
SGSGLTIKLPDKKEESQDFCYFTNCGQTCPSGYTEIPRGDKDSQIMLDATECLAGQDQVQ
TLCCPKSSKVPKCRWRGYQGNDHCPVGCNAGEVAVGTHHQGCKKSGWQTACCDATDSTGP
WSKCGWTADCYDDDDSTCPKGFSSFVVGSRGGFGGQKSCKKGKKYNYCCTETPKAFKNCE
WVGHEVSFPNEQACTNTCPHGSTRIAAQDISTSWSTSGYLAHTDKCTYGFEAYCCAGEKE
SDKDERDIIEYQDKDAKEFDYALKRFLRDPVCPDEEIEFGSDDGLSIEEGLSARNILLGR
ATDNSAVLAVLLPIMGVWVTSQNPRLDLTQIYNRDIEDAGFSETAANLTTYRDLLYQSDW
TGRPRYSGRAVARMALCDLAESREGLDNLATVPAALCEVPSSTGSEAHKRDIQARTINVN
VMTDRGRGNVQPSAAYIFKAIKAGHLSLHYLRWLQSTGQVILEVAYWIGPSPGTEDPANS
YRNQYRDRDHRNAVDRWVIFHFHIPLDSNTFWTEPSGVNDYYLGVSSFDMYHSQGVHRPN
PPRGYRGPVDFRAEWVYSSSYARGSSNTGPLTDYNRRREPFNCRIPEDGPPPGPAFYLGR
DYTSQINDLLTENRPAGLAILINDFGIQLHRAGIFRSANLAMIWPRAANGNLPPAGSSWG
DQEYRPTAQAFQINFDLNGARVNNVQNADP

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	117	464	3.5e-63	0.956081081081081

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	2.52e-71	119	459	1	334	Glyco_18 domain.
395573	Glyco_hydro_18	1.14e-67	119	459	1	307	Glycosyl hydrolases family 18.
119357	GH18_zymocin_alpha	5.26e-67	121	459	3	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	1.06e-61	120	460	1	342	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	2.04e-51	120	459	1	322	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
QKD59080.1|CBM18|GH18	0.0	1	1170	1	1173
QKD61252.1|CBM18|GH18	0.0	1	1170	1	1173
CEF84382.1|CBM18|GH18	0.0	1	1170	1	1159
CZS74851.1|CBM18|GH18	0.0	2	1170	30	1177
APA07677.1|CBM18|GH18	0.0	21	1168	17	1164

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5WUS_A	1.90e-34	119	468	3	351	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	4.69e-34	118	460	4	351	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
1HJV_A	1.14e-33	119	465	2	342	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]
5XEP_A	1.24e-33	114	460	18	359	Crystal structure of BRP39, a chitinase-like protein, at 2.6 Angstorm resolution [Mus musculus],5XEP_B Crystal structure of BRP39, a chitinase-like protein, at 2.6 Angstorm resolution [Mus musculus],5XEP_C Crystal structure of BRP39, a chitinase-like protein, at 2.6 Angstorm resolution [Mus musculus],5XEP_D Crystal structure of BRP39, a chitinase-like protein, at 2.6 Angstorm resolution [Mus musculus],5XEP_E Crystal structure of BRP39, a chitinase-like protein, at 2.6 Angstorm resolution [Mus musculus],5XEP_F Crystal structure of BRP39, a chitinase-like protein, at 2.6 Angstorm resolution [Mus musculus]
1SR0_A	1.51e-33	119	465	2	341	Crystal structure of signalling protein from sheep(SPS-40) at 3.0A resolution using crystal grown in the presence of polysaccharides [Ovis aries],1ZBK_A Recognition of specific peptide sequences by signalling protein from sheep mammary gland (SPS-40): Crystal structure of the complex of SPS-40 with a peptide Trp-Pro-Trp at 2.9A resolution [Ovis aries],1ZL1_A Crystal structure of the complex of signalling protein from sheep (SPS-40) with a designed peptide Trp-His-Trp reveals significance of Asn79 and Trp191 in the complex formation [Ovis aries],2DPE_A Crystal structure of a secretory 40KDA glycoprotein from sheep at 2.0A resolution [Ovis aries],2DSU_A Binding of chitin-like polysaccharide to protective signalling factor: Crystal structure of the complex formed between signalling protein from sheep (SPS-40) with a tetrasaccharide at 2.2 A resolution [Ovis aries],2DSV_A Interactions of protective signalling factor with chitin-like polysaccharide: Crystal structure of the complex between signalling protein from sheep (SPS-40) and a hexasaccharide at 2.5A resolution [Ovis aries],2DSW_A Binding of chitin-like polysaccharides to protective signalling factor: crystal structure of the complex of signalling protein from sheep (SPS-40) with a pentasaccharide at 2.8 A resolution [Ovis aries],2FDM_A Crystal structure of the ternary complex of signalling glycoprotein frm sheep (SPS-40)with hexasaccharide (NAG6) and peptide Trp-Pro-Trp at 3.0A resolution [Ovis aries],2G41_A Crystal structure of the complex of sheep signalling glycoprotein with chitin trimer at 3.0A resolution [Ovis aries],2G8Z_A Crystal structure of the ternary complex of signalling protein from sheep (SPS-40) with trimer and designed peptide at 2.5A resolution [Ovis aries]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	9.78e-43	64	458	317	711	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|Q9WTV1|CH3L1_RAT	8.35e-36	114	465	16	361	Chitinase-3-like protein 1 OS=Rattus norvegicus OX=10116 GN=Chi3l1 PE=2 SV=3
sp|Q9D7Q1|CHIT1_MOUSE	1.04e-33	138	467	43	369	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
sp|Q5RBP6|CH3L1_PONAB	1.82e-33	116	465	47	390	Chitinase-3-like protein 1 OS=Pongo abelii OX=9601 GN=CHI3L1 PE=2 SV=1
sp|Q61362|CH3L1_MOUSE	3.02e-33	114	460	26	367	Chitinase-3-like protein 1 OS=Mus musculus OX=10090 GN=Chi3l1 PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000193	0.999773	CS pos: 22-23. Pr: 0.9760

TMHMM  Annotations     

There is no transmembrane helices in FPRN_13180-t42_1-p1.