CAZyme Information: ASPGLDRAFT_121816-t33_1-p1

Basic Information

• Species: Aspergillus glaucus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus glaucus
• CAZyme ID: ASPGLDRAFT_121816-t33_1-p1
• CAZy Family: AA3
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1086		116757.78	4.0986

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AglaucusCBS516.65	11429	1160497	175	11254

• Gene Location: location=KV878892:8314-12041(-)

Full Sequence      

MLSFSSSWLLLSLLVLNNVIPSALAAMGSCSSTDKCESGCCSKEGYCGFGPDFCGDDVCI
SGCDAIAECGEFAKVNGTECPLNVCCSEFGFCGTTEEFCGTGCQSGCDPVNEPSCGGTSS
EARYIGYYEGWNTQRQCDTVTPDNINVVPWTHLYYSFAYIDKSDFTITTMNDGDEDYWTE
FTALKKKKSSLKTYLSIGGWDLGGEIWSNLCRFPGTRSAFIKSVVSTMKKYDFDGIDIDW
EYPAAEDRGGASRNTANLVTLLKELREEVKTTYGITVTLPSSYWYLKGFDLKGMAEYLDI
FNFMSYDIHGTWDGSTKWTQSVVNPHTNLTEVSTGLDLLWRNNIDPSKVLLGLGFYGRSF
GLDDPSCTSPGCAFDKDHNSTGGAAAGECTATSGILSDYEINRIIESNEPTIEYDEEAAV
NWMTWNSNQWVSFDNERTLKQKADFANSRCMGGLFSWALDMGGPGSLKSPNSMDTSDTSM
DGADVEGGSDGTETLFVGSGVFDSDSNQVTAIGPVNIVFPSTTLATPTTIPAQGLPTSVE
VAWKTTKTVTSESITTATTTITRYIQHTTISVPPLTTNAHGFHNWNITEANATQLVGTLW
PSIPLPPVTITDDPNPLKETGVSHPAITRTVHLPPWPWYTDNENPSKVTFTQGNPPGPTC
TANCGQVCTEFCGGPCLNNCDDLSYSDFVDPIDNNPPSVAPCSGPDCKNGKCIGKLCVQK
GCTGKDCYSGICVGGDDCKPTGCTGSDCDSGHCSGSDCQDHGCVGSDCDSSSGGCFGIGC
LSWGCLGSQCSSHDFTCTGPNCRVVSCIGEDCKNGICTGKDCQSEDSDCETQEAEMCTDW
ISSTLVTPASTYSTETLTTACETITACNAKPTTATKTIDGDDFIEATVTIIEYEETLDAD
IEASIESDWSSYISSYWSAIDSTSTSTTATKTTTEGGGTDPTDSAIPNSFIIFKYHEEKD
NGFDLSHSDSYAFYGAYYSYRQQITEDDVCAHTRKVTNSVGAKGSTEYPTDLGSFTLGQY
TGCKYTPNGSKPGIVSCDNNELPFECIGYIHTGSGNVVDYYCGQTMSGSGTRTFRSYNKA
VECLVY

Enzyme Prediction     

EC	3.2.1.14:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	122	461	1.5e-69	0.9324324324324325

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
214753	Glyco_18	3.26e-73	125	461	3	333	Glyco_18 domain.
119357	GH18_zymocin_alpha	1.13e-72	125	462	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.
395573	Glyco_hydro_18	7.85e-69	123	461	1	306	Glycosyl hydrolases family 18.
119351	GH18_chitolectin_chitotriosidase	1.30e-68	127	461	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.
119365	GH18_chitinase	5.93e-57	125	461	2	321	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
BAE65677.1|GH18	0.0	152	1086	24	982
CAP74296.1|CBM18|GH18	7.68e-281	18	869	18	885
QSS62098.1|CBM18|GH18	1.49e-208	23	654	31	673
QSS71211.1|GH18	1.08e-157	170	710	1	648
BCS02338.1|CBM18|GH18	8.08e-124	30	461	56	490

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JM7_A	4.67e-46	125	460	7	348	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
6JM8_A	5.32e-45	125	460	7	348	Crystal structure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
5WUS_A	9.10e-45	121	461	1	341	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]
2YBT_A	6.22e-44	127	461	10	347	Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_B Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_C Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_D Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_E Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBT_F Crystal structure of human acidic chitinase in complex with bisdionin C [Homo sapiens],2YBU_A Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_B Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_C Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_D Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_E Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens],2YBU_F Crystal structure of human acidic chitinase in complex with bisdionin F [Homo sapiens]
5WUP_A	6.29e-44	123	461	94	437	Crystal structure of a insect group III chitinase (CAD1) from Ostrinia furnacalis [Ostrinia furnacalis],5WV9_A Crystal structure of a insect group III chitinase complex with (GlcNAc)6 (CAD1-(GlcNAc)6) from Ostrinia furnacalis [Ostrinia furnacalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6RY07|CHIA_RAT	1.22e-42	125	461	25	364	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|Q9BZP6|CHIA_HUMAN	7.83e-42	127	461	27	364	Acidic mammalian chitinase OS=Homo sapiens OX=9606 GN=CHIA PE=1 SV=1
sp|Q13231|CHIT1_HUMAN	8.76e-42	120	461	20	362	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|P36362|CHIT_MANSE	1.20e-41	118	461	19	374	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
sp|Q91XA9|CHIA_MOUSE	1.35e-41	125	461	25	364	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
0.000226	0.999738	CS pos: 25-26. Pr: 0.9654

TMHMM  Annotations     

There is no transmembrane helices in ASPGLDRAFT_121816-t33_1-p1.