CAZyme Information: EEP77206.1

Basic Information

• Species: Uncinocarpus reesii
• Lineage: Ascomycota; Eurotiomycetes; ; Onygenaceae; Uncinocarpus; Uncinocarpus reesii
• CAZyme ID: EEP77206.1
• CAZy Family: GH132
• CAZyme Description: Chitinase [Source:UniProtKB/TrEMBL;Acc:C4JK98]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
828		89272.36	7.4203

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ureesii1704	7856	336963	96	7760

• Gene Location: location=CH476615:5363729-5366723(+)

Full Sequence      

MTLVPESDIDLGLFKAFTGLKKRKPSLKTFISVGGWDAGGRIFTTMAHRASYRKAFIKSA
VKLMDKYGFDGIDIDWEYPVAWERGYLKGFDIQRLERYVDWFNFMSYDIHEIEAGLDLLW
RNGVDPGVVSLGLGFYGRSFTLKDPGCNQPGCAFIRRGRASGGAKAGECTGQSGVLSNYE
INRILKSKSLTPASDQEAAVKWISWDSDQWVSYDDAETLRRKGEFANARCLGGTFAWALD
LGGPGTLGRPETLNGSDLEGANPDGSDSGSGDVFISPNIFTESEPNIACVAPCTFILPPI
PLGSSTTISFPPYSTSLEVAWPTTITITLPGGAVSTSTGLGRTILNTTLTIPPVTTTVIE
VWNWILTDIEVTSTSHKITSSILPPPFVITDNQTVITVTRPVESTSGTTSTTDVVPPVTV
ITRPVTTRTITPPPFPWWSVNPVESPLPTLTYTQGPPSPLCEGDDCGKKCKKFCKEPCRY
DCKDGDDFLDQNDRDRDRDVERRRCEGPDCSNGECAGIFCVTFGCIGFDCVDGICLGPLC
KITTCTGSDCRKGRCIGPKCRTGSGCAGDDCSSNGRCIGPKCISFGCIGADCKPCSGSSC
SGGWECTGPRCKIVTCKGSSCRNGLCSGSGCEPGNDGCDEAQTARRCTEMVSKVRPPKET
TYSTTTSTICSTITACDAQPTTVTTTYSRDGIKTQRREVITYKKYKENPAQAACMKKALQ
IRRDNLSKLMFEPQNTPTTTRKRPEPTGPVEQKYSCKGSIRCKSAIKLGSDCQMAKAALV
ENTLYGNTPRCVSGGTCYAAPERSFMGCGVMVQGPEGKCELTGNQIAA

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	90	240	1e-25	0.47635135135135137

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119351	GH18_chitolectin_chitotriosidase	1.43e-63	5	241	49	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	7.76e-60	7	241	47	333	Glyco_18 domain.
395573	Glyco_hydro_18	4.21e-51	4	240	40	305	Glycosyl hydrolases family 18.
119365	GH18_chitinase	6.14e-41	10	240	68	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.
119357	GH18_zymocin_alpha	3.49e-36	4	242	46	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSS71211.1|GH18	4.22e-161	10	740	5	871
QSS62098.1|CBM18|GH18	2.74e-148	2	469	175	783
BAE65677.1|GH18	1.01e-123	10	692	46	781
CAP74296.1|CBM18|GH18	4.23e-119	2	510	166	725
BCS04473.1|CBM18|CBM50|GH18	1.08e-73	2	390	174	603

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JM7_A	6.85e-34	1	261	50	375	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
6JM8_A	7.62e-33	1	261	50	375	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
1HKK_A	1.84e-30	10	241	52	341	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1HKI_A	1.88e-30	10	241	52	341	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	1.88e-30	10	241	52	341	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|Q13231|CHIT1_HUMAN	4.68e-29	10	241	73	362	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q91XA9|CHIA_MOUSE	7.50e-27	10	241	73	364	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2
sp|Q95M17|CHIA_BOVIN	2.39e-26	10	241	73	364	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q9D7Q1|CHIT1_MOUSE	3.92e-26	13	241	76	360	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
sp|Q6TMG6|CH3L1_SHEEP	2.43e-25	10	241	52	334	Chitinase-3-like protein 1 OS=Ovis aries OX=9940 GN=CHI3L1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000077	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EEP77206.1.