CAZyme Information: EAQ84573.1

Basic Information

• Species: Chaetomium globosum
• Lineage: Ascomycota; Sordariomycetes; ; Chaetomiaceae; Chaetomium; Chaetomium globosum
• CAZyme ID: EAQ84573.1
• CAZy Family: AA9
• CAZyme Description: Chitinase [Source:UniProtKB/TrEMBL;Acc:Q2GTW7]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1749	CH408034|CGC3	192210.47	4.8111

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CglobosumCBS148.51	11232	306901	184	11048

• Gene Location: location=CH408034:763131-768777(-)

Full Sequence      

MRYPIVLALLCGGRLAEALPWHQATDHSAVPAVADVPRTCRNPVLPFDYSAKVRREYELP
LCRDGDEKLGITPFLGAMDAPSLLSGRATVDDYTCAPDRPCANKACCPKATLSCNYGEEA
CGTSGISPNEVCWSNCDAKSECGKDAKVPGQECPLNVCCGKWGFCGMTEDYCDKEDHGAT
GGCQSNCDQPGPKNKASTQARVIGYYEGWRADSACQGMGLNDIPVNSLTHLYFSFASITP
DTYSIAPMEGIDGSLFSKFTNLKKKNPALKTVIAIGGWTFNDPGPTQKVFSNMVSTAENR
ETFIDNLFSFLREYAFDGVDFDWEYPGADDRGGVEADGKNFVTFLKELDAANKKQPVKYV
VSFTLPTSYWYMRHFDLKAVDHVDFVNVMSYDLHGVWDGKNPIGQKIYGHTNITEMKQAF
DLFWRNDVPANKLNMGLGFYGRAFQLQDPSCSKPGCGFKGGATKGGCSGESGILSYREIM
AVIDSKKIKPVHDKKAGVKYITWNNDQWVSYDDADTFKQKKDLAADLGLGGYLIWAIDQD
DEHLTALQAVISPKKLGDLGAASDKDDWQSSNKHCYITSCDGNCDAGDIKITDQPCGEDD
KRSKLCCPLSGAPDPKECTWRGNPTLCNGHCHDDEVMMEMNKWGDGGGCSDGNKAYCCKS
PLAAENTCYWTGVGGSCNGDDLPLTFSGTVLTILEDVAKVILRVVGRAYPLTALAGEALL
LVLDELDLDTDKYYCCPKEDIPKWKNCDWFGKPGSCYDGHCPDMTYAQLTDSYFGGGETC
GWQLSRVRTFCCEPAKDPLFLPVPLGNLFENPPEGESVDTDFSLETDKDSDSQQNPNDAA
FQFVVLASPEELQVSLDKRDGSHWDIFSGCDSAIGEDGPHTVQMVCTDFSEGSNCHKISL
GHGVPGTILQMPPGCGPGKYAVAKDMVPTSDPAKTILPRHLEHLSAAHTAVVYDLTFDYD
FTRVRRDLGDTQMRIDFSNQDDYWDTIVAAAGNTKKKIKRSLADTGGNHARWLEEEFRDD
YHFGTLSRRDLEERWFGSGVLDWLARLVKPEIKREFTYNYRDTLTAKLVDETWQCNRNGV
DYEGHILAQALLKVNVATSFGFTLIVTKLTPPLDISQSYLTFYNKGEITGVLTLEAVAKF
SFHKSEVILNIPFPGASFKIPGIATIGPQLTVEGSIDASLTLAGKVETRLEFANWEVRQV
LPDNGDSNYTPKEIGDGDPDLKRTGDNKDLDEPNFYAGVQALGDVTAKISAAAEFGIRFD
KRWDIDPAAAAIVAEASVMLKMGAGISTKDTCPFTFGVDVGARLFARATAPGFGWPGAEV
AITPAYNKPIIDGGRCPGLGPLPTKRDLTLLTIEANDTSGHRACVGPGTTCSQIGYAWPE
SSEDPEDSSLLRRGGTFGKVLEKRARKEVHICDQTFTFLYPSNSVAKSKGNLPYGFTTTD
CADFNFDALGINGVAGVSYDTEHVLEAQLIKLFFDEVDHDNFNGFPHPDPTQPATTRLGF
CELVNVLWDINPVVIPNLESAFTGQALSPYEQVVAQFPTTTWKVDEYVRLEKNINSPAKA
NAWGDNQVADFDKWIGGDPNDYGSDVNLDTPVYTGLITTLEGAEKIMKSMRAILGSRLYH
NHPTIMAILRAQKARVGEVLRRLDTEILPNNPPQAGWTPWAPMGLKDKWDAFMRGKMALA
VTKSDKVLNDILPRMQVQWATQAHRDAAADDSNDTQAERLVKARKRRLINTIDAFAEALR
LAPPWQWAF

Enzyme Prediction     

No EC number prediction in EAQ84573.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	199	545	2.2e-72	0.956081081081081

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	1.26e-91	201	540	1	334	Glyco_18 domain.
119351	GH18_chitolectin_chitotriosidase	2.99e-83	229	541	29	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.
395573	Glyco_hydro_18	1.49e-80	201	540	1	307	Glycosyl hydrolases family 18.
119357	GH18_zymocin_alpha	8.75e-80	203	538	3	343	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.
119365	GH18_chitinase	5.54e-70	202	540	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
ATY59023.1|CBM18|GH18	0.0	33	1745	30	1836
QPG94581.1|CBM18|GH18	0.0	28	1745	32	1839
QVM13519.1|CBM18|GH18	0.0	27	1749	32	1761
CBX95390.1|CBM18|GH18	0.0	37	1708	38	1744
UQC79223.1|CBM18|GH18	0.0	39	1726	48	1759

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HKK_A	3.46e-54	200	541	1	343	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1HKI_A	3.56e-54	200	541	1	343	Crystal structure of human chitinase in complex with glucoallosamidin B [Homo sapiens],1HKJ_A Crystal structure of human chitinase in complex with methylallosamidin [Homo sapiens],1HKM_A High resolution crystal structure of human chitinase in complex with demethylallosamidin [Homo sapiens]
1LG1_A	3.56e-54	200	541	1	343	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	4.90e-54	200	541	1	343	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]
1GUV_A	4.96e-54	200	541	1	343	Structure of human chitotriosidase [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	5.66e-54	115	543	286	725	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	2.29e-52	200	541	22	364	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q9D7Q1|CHIT1_MOUSE	5.40e-44	222	541	45	362	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
sp|Q95M17|CHIA_BOVIN	9.50e-43	229	541	52	366	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q91XA9|CHIA_MOUSE	1.31e-42	202	541	24	366	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000211	0.999759	CS pos: 18-19. Pr: 0.9701

TMHMM  Annotations     

There is no transmembrane helices in EAQ84573.1.